- published: 25 Jun 2020
- views: 184
-
remove the playlistFragment Crystallizable Region
- remove the playlistFragment Crystallizable Region
Fragment crystallizable region
The fragment crystallizable region (Fc region) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system. In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (CH domains 2–4) in each polypeptide chain. The Fc regions of IgGs bear a highly conserved N-glycosylation site.Glycosylation of the Fc fragment is essential for Fc receptor-mediated activity. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6 linked sialic acid residues.
The other part of an antibody, called the Fab region, contains variable sections that define the specific target that the antibody can bind. By contrast, the Fc region of all antibodies in a class are the same for each species; they are constant rather than variable. The Fc region is, therefore, sometimes incorrectly termed the "fragment constant region".
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Fragment_crystallizable_region
Ü (region)
Ü (Tibetan: དབུས་, Wylie: dbus, ZYPY: Wü ; pronounced w-yu, similar to English word "we") is a geographic division and a historical region in Tibet. Together with Tsang (Tib. གཙང་, gtsang), it forms Central Tibet Ü-Tsang (Tib. དབུས་གཙང་, Wyl. dbus gtsang), which is one of the three Tibetan regions or cholka (cholka-sum). The other two cholka are Kham (Tib. ཁམས་, Wyl. khams) (Dotod) and Amdo (Tib. ཨ༌མདོ;Wyl. a mdo) (Domed). According to a Tibetan saying, "the best religion comes from Ü-Tsang, the best men from Kham, and the best horses from Amdo".
Constituent districts
Taken together, Ü and Tsang are considered to be the center of Tibetan civilization, from historical, cultural, political and economic perspectives. They are centered on the valley of the Yarlung Tsangpo River, which flows eastward at about 3,600 metres (11,800 ft) above sea level. Of this territory, Ü constitutes the eastern portion, up to Sokla Kyao in the east where it borders to Kham. It includes the Lhasa River valley system, where Lhasa is situated, and the Yarlung and Chonggye valleys to the south of the Tsangpo.
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Ü_(region)
List of regions of Quebec
The province of Quebec, Canada, is officially divided into 17 administrative regions. Traditionally (and unofficially), it is divided into around twenty regions. As of the 2011 Canadian Census, the population of Quebec was 7,903,001, the land area was 1,356,547.02 km2 and the population density was 5.8 inhabitants per square kilometre.
Administrative
Administrative regions are used to organize the delivery of provincial government services. They are also the basis of organization for regional conferences of elected officers (French: conférences régionales des élus, CRÉ), with the exception of the Montérégie and Nord-du-Québec regions, which each have three CRÉs or equivalent bodies. (In the Nord-du-Québec region, the Kativik Regional Government and Cree Regional Authority, in addition to their other functions, play the role of a CRÉ).
List
The subregions of Montérégie and Nord-du-Québec have their own regional conference of elected officers (CRÉ). Municipalities with 20,000-plus populations in the 2011 Census are listed, with those 50,000 or over bolded. In addition, the seat of the relevant CRÉ is indicated, as well as other major cities and towns. If the population of a CRÉ is less than 20,000, it is shown in italics.
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/List_of_regions_of_Quebec
Region (mathematics)
In mathematical analysis, the word region usually refers to a subset of 
or 
that is open (in the standard Euclidean topology), connected and non-empty. A closed region is sometimes defined to be the closure of a region.
Regions and closed regions are often used as domains of functions or differential equations.
According to Kreyszig,
According to Yue Kuen Kwok,
See also
Notes and references
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Region_(mathematics)
Podcasts:
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fragment crystallizable region (English) - Medical terminology for medical students -
(Fc fragment) The tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system. Cf. pFc' fragment, antigen-binding fragment, F(ab')2 fragment, Fab' fragment
published: 25 Jun 2020 -
Antibodies: Structures, types and functions
the antibody structures including heavy chain and light chain are illustrated briefly in this video there are five types of antibodies. do you know them ? there are three major functions of antibodies. do you know them?
published: 02 Sep 2019 -
Fab, Fc and F(ab')2 in antibodies (immunoglobulins) (FL-Immuno/36)
This video lecture explains the origin and significance of terms Fab Fc F(ab')2 We have discussed in brief the key experiments revealing the antibody structure.
published: 10 Jun 2017 -
Fc receptors
This video presents the receptors that bind the constant region of antibodies - Fc receptors, including the Fc-gamma receptors and Fc-epsilon receptors.
published: 01 Oct 2017 -
Antibody
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by inhibiting a part of a microbe that is essentia...
published: 14 Sep 2020 -
Immunology - Antibody Structure & Function
Antibodies, also known as immunoglobulins, are like the ammunition of the body’s humoral defense against microorganisms. Plasma cells are like the turret guns of the immune system that secrete thousands of antibodies per second. You should know the general structure of the 5 types of antibodies, as well as the specific structure of an individual antibody. First, I’m going to draw a 2 by 2 grid to demonstrate the difference between the light and heavy chains, as well as the variable and constant regions. Each antibody has 2 light chains with a variable region known as V-L and a constant region known as C-L. Each heavy has a variable region known as V-H and three constant regions known as C-H-1, C-H-2, and C-H-3. Disulfide bonds join the light chain to the heavy chain here, and the heavy ch...
published: 24 Jul 2016 -
تركيب الجسم المضاد (بأختصار)
يشمل هذا المقطع المواضيع التالية: -Heavy and light chains -Fab fragment -Hypervariable region -Fc fragment
published: 24 Jul 2021 -
fragment antigen binding region (English) - Medical terminology for medical students -
(Fab region) A region on an antibody that binds to an antigen. Cf. complementarity-determining region
published: 26 Jun 2020
developed with YouTube
0:37
fragment crystallizable region (English) - Medical terminology for medical students -
- Order: Reorder
- Duration: 0:37
- Uploaded Date: 25 Jun 2020
- views: 184
(Fc fragment)
The tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This pr...
(Fc fragment)
The tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system.
Cf. pFc' fragment, antigen-binding fragment, F(ab')2 fragment, Fab' fragment
https://wn.com/Fragment_Crystallizable_Region_(English)_Medical_Terminology_For_Medical_Students
(Fc fragment)
The tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system.
Cf. pFc' fragment, antigen-binding fragment, F(ab')2 fragment, Fab' fragment
2:33
Antibodies: Structures, types and functions
- Order: Reorder
- Duration: 2:33
- Uploaded Date: 02 Sep 2019
- views: 72041
the antibody structures including heavy chain and light chain are illustrated briefly in this video
there are five types of antibodies. do you know them ?
there...
the antibody structures including heavy chain and light chain are illustrated briefly in this video
there are five types of antibodies. do you know them ?
there are three major functions of antibodies. do you know them?
https://wn.com/Antibodies_Structures,_Types_And_Functions
the antibody structures including heavy chain and light chain are illustrated briefly in this video
there are five types of antibodies. do you know them ?
there are three major functions of antibodies. do you know them?
- published: 02 Sep 2019
- views: 72041
6:33
Fab, Fc and F(ab')2 in antibodies (immunoglobulins) (FL-Immuno/36)
- Order: Reorder
- Duration: 6:33
- Uploaded Date: 10 Jun 2017
- views: 80562
This video lecture explains the origin and significance of terms
Fab
Fc
F(ab')2
We have discussed in brief the key experiments revealing the antibody structur...
This video lecture explains the origin and significance of terms
Fab
Fc
F(ab')2
We have discussed in brief the key experiments revealing the antibody structure.
https://wn.com/Fab,_Fc_And_F(Ab')2_In_Antibodies_(Immunoglobulins)_(Fl_Immuno_36)
This video lecture explains the origin and significance of terms
Fab
Fc
F(ab')2
We have discussed in brief the key experiments revealing the antibody structure.
- published: 10 Jun 2017
- views: 80562
9:32
Fc receptors
- Order: Reorder
- Duration: 9:32
- Uploaded Date: 01 Oct 2017
- views: 25858
This video presents the receptors that bind the constant region of antibodies - Fc receptors, including the Fc-gamma receptors and Fc-epsilon receptors.
This video presents the receptors that bind the constant region of antibodies - Fc receptors, including the Fc-gamma receptors and Fc-epsilon receptors.
https://wn.com/Fc_Receptors
This video presents the receptors that bind the constant region of antibodies - Fc receptors, including the Fc-gamma receptors and Fc-epsilon receptors.
- published: 01 Oct 2017
- views: 25858
4:17
Antibody
- Order: Reorder
- Duration: 4:17
- Uploaded Date: 14 Sep 2020
- views: 83168
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutra...
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by inhibiting a part of a microbe that is essential for its invasion and survival). Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance. The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region (located at the base of the "Y"), which contains a conserved glycosylation site involved in these interactions.[4] The production of antibodies is the main function of the humoral immune system.[5]
Antibodies are secreted by B cells of the adaptive immune system, mostly by differentiated B cells called plasma cells. Antibodies can occur in two physical forms, a soluble form that is secreted from the cell to be free in the blood plasma, and a membrane-bound form that is attached to the surface of a B cell and is referred to as the B-cell receptor (BCR). The BCR is found only on the surface of B cells and facilitates the activation of these cells and their subsequent differentiation into either antibody factories called plasma cells or memory B cells that will survive in the body and remember that same antigen so the B cells can respond faster upon future exposure. In most cases, interaction of the B cell with a T helper cell is necessary to produce full activation of the B cell and, therefore, antibody generation following antigen binding. Soluble antibodies are released into the blood and tissue fluids, as well as many secretions to continue to survey for invading microorganisms.
https://wn.com/Antibody
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by inhibiting a part of a microbe that is essential for its invasion and survival). Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance. The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region (located at the base of the "Y"), which contains a conserved glycosylation site involved in these interactions.[4] The production of antibodies is the main function of the humoral immune system.[5]
Antibodies are secreted by B cells of the adaptive immune system, mostly by differentiated B cells called plasma cells. Antibodies can occur in two physical forms, a soluble form that is secreted from the cell to be free in the blood plasma, and a membrane-bound form that is attached to the surface of a B cell and is referred to as the B-cell receptor (BCR). The BCR is found only on the surface of B cells and facilitates the activation of these cells and their subsequent differentiation into either antibody factories called plasma cells or memory B cells that will survive in the body and remember that same antigen so the B cells can respond faster upon future exposure. In most cases, interaction of the B cell with a T helper cell is necessary to produce full activation of the B cell and, therefore, antibody generation following antigen binding. Soluble antibodies are released into the blood and tissue fluids, as well as many secretions to continue to survey for invading microorganisms.
- published: 14 Sep 2020
- views: 83168
3:26
Immunology - Antibody Structure & Function
- Order: Reorder
- Duration: 3:26
- Uploaded Date: 24 Jul 2016
- views: 34563
Antibodies, also known as immunoglobulins, are like the ammunition of the body’s humoral defense against microorganisms. Plasma cells are like the turret guns o...
Antibodies, also known as immunoglobulins, are like the ammunition of the body’s humoral defense against microorganisms. Plasma cells are like the turret guns of the immune system that secrete thousands of antibodies per second. You should know the general structure of the 5 types of antibodies, as well as the specific structure of an individual antibody.
First, I’m going to draw a 2 by 2 grid to demonstrate the difference between the light and heavy chains, as well as the variable and constant regions. Each antibody has 2 light chains with a variable region known as V-L and a constant region known as C-L. Each heavy has a variable region known as V-H and three constant regions known as C-H-1, C-H-2, and C-H-3. Disulfide bonds join the light chain to the heavy chain here, and the heavy chains of IgG to each other here. These disulfide bonds bend here at the Hinge region so that the overall antibody structure forms a Y shape.
Four regions, V-L, C-L, V-H, and C-H-1 make up the fragment of antigen binding, or Fab. The variable regions of the Fab fragment determine the specific idiotype: the unique structure of which binds to a corresponding specific antigen. Each B cell expresses only one idiotype of an antibody. As an example, a lab-made immune Fab specific to digoxin is used as an antidote to overdoses of the medication.
C-H-2 and C-H-3 together make up the Fc region of the antibody, which corresponds to the stalk of the Y. C-H-2 has the special property of binding to complement, something I will cover in a future video.
Now let’s discuss the different isotypes of immunoglobulins. There are 5 types: IgG, IgE, IgD, IgM, and IgA. They are differentiated biochemically by their Fc regions and their different functions. All have monomer forms, but only IgA and IgM have different forms when secreted. IgM can exist as a pentamer linked together by disulfide bonds and a J chain, or joining chain. IgA can exist as a dimer with a J chain as well as a Secretory protein. If you were to know just very simple associations to each type then know these. IgM – Immediate response. IgG – delayed response. IgA – mucous membranes. IgE – allergies and parasites. IgD – unclear function.
Question: how many binding sites exist on secreted IgM? Think carefully! Most people’s initial reaction is to say five because secretory IgM exists as a pentamer. However, it is important to remember that each antibody monomer has two binding sites, and thus, secretory IgM has 2 times 5 = 10 binding sites.
Thanks for watching! Be sure to like and subscribe for more.
https://wn.com/Immunology_Antibody_Structure_Function
Antibodies, also known as immunoglobulins, are like the ammunition of the body’s humoral defense against microorganisms. Plasma cells are like the turret guns of the immune system that secrete thousands of antibodies per second. You should know the general structure of the 5 types of antibodies, as well as the specific structure of an individual antibody.
First, I’m going to draw a 2 by 2 grid to demonstrate the difference between the light and heavy chains, as well as the variable and constant regions. Each antibody has 2 light chains with a variable region known as V-L and a constant region known as C-L. Each heavy has a variable region known as V-H and three constant regions known as C-H-1, C-H-2, and C-H-3. Disulfide bonds join the light chain to the heavy chain here, and the heavy chains of IgG to each other here. These disulfide bonds bend here at the Hinge region so that the overall antibody structure forms a Y shape.
Four regions, V-L, C-L, V-H, and C-H-1 make up the fragment of antigen binding, or Fab. The variable regions of the Fab fragment determine the specific idiotype: the unique structure of which binds to a corresponding specific antigen. Each B cell expresses only one idiotype of an antibody. As an example, a lab-made immune Fab specific to digoxin is used as an antidote to overdoses of the medication.
C-H-2 and C-H-3 together make up the Fc region of the antibody, which corresponds to the stalk of the Y. C-H-2 has the special property of binding to complement, something I will cover in a future video.
Now let’s discuss the different isotypes of immunoglobulins. There are 5 types: IgG, IgE, IgD, IgM, and IgA. They are differentiated biochemically by their Fc regions and their different functions. All have monomer forms, but only IgA and IgM have different forms when secreted. IgM can exist as a pentamer linked together by disulfide bonds and a J chain, or joining chain. IgA can exist as a dimer with a J chain as well as a Secretory protein. If you were to know just very simple associations to each type then know these. IgM – Immediate response. IgG – delayed response. IgA – mucous membranes. IgE – allergies and parasites. IgD – unclear function.
Question: how many binding sites exist on secreted IgM? Think carefully! Most people’s initial reaction is to say five because secretory IgM exists as a pentamer. However, it is important to remember that each antibody monomer has two binding sites, and thus, secretory IgM has 2 times 5 = 10 binding sites.
Thanks for watching! Be sure to like and subscribe for more.
- published: 24 Jul 2016
- views: 34563
7:55
تركيب الجسم المضاد (بأختصار)
- Order: Reorder
- Duration: 7:55
- Uploaded Date: 24 Jul 2021
- views: 2771
يشمل هذا المقطع المواضيع التالية:
-Heavy and light chains
-Fab fragment
-Hypervariable region
-Fc fragment
يشمل هذا المقطع المواضيع التالية:
-Heavy and light chains
-Fab fragment
-Hypervariable region
-Fc fragment
https://wn.com/تركيب_الجسم_المضاد_(بأختصار)
يشمل هذا المقطع المواضيع التالية:
-Heavy and light chains
-Fab fragment
-Hypervariable region
-Fc fragment
- published: 24 Jul 2021
- views: 2771
0:22
fragment antigen binding region (English) - Medical terminology for medical students -
- Order: Reorder
- Duration: 0:22
- Uploaded Date: 26 Jun 2020
- views: 191
(Fab region)
A region on an antibody that binds to an antigen.
Cf. complementarity-determining region
(Fab region)
A region on an antibody that binds to an antigen.
Cf. complementarity-determining region
https://wn.com/Fragment_Antigen_Binding_Region_(English)_Medical_Terminology_For_Medical_Students
(Fab region)
A region on an antibody that binds to an antigen.
Cf. complementarity-determining region
- published: 26 Jun 2020
- views: 191
0:37
fragment crystallizable region (English) - Medical terminology for medical students -
(Fc fragment)
The tail region of an antibody that interacts with cell surface receptors c...
published: 25 Jun 2020
fragment crystallizable region (English) - Medical terminology for medical students -
fragment crystallizable region (English) - Medical terminology for medical students -
- Report rights infringement
- published: 25 Jun 2020
- views: 184
(Fc fragment)
The tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system.
Cf. pFc' fragment, antigen-binding fragment, F(ab')2 fragment, Fab' fragment
2:33
Antibodies: Structures, types and functions
the antibody structures including heavy chain and light chain are illustrated briefly in t...
published: 02 Sep 2019
Antibodies: Structures, types and functions
Antibodies: Structures, types and functions
- Report rights infringement
- published: 02 Sep 2019
- views: 72041
the antibody structures including heavy chain and light chain are illustrated briefly in this video
there are five types of antibodies. do you know them ?
there are three major functions of antibodies. do you know them?
6:33
Fab, Fc and F(ab')2 in antibodies (immunoglobulins) (FL-Immuno/36)
This video lecture explains the origin and significance of terms
Fab
Fc
F(ab')2
We have ...
published: 10 Jun 2017
Fab, Fc and F(ab')2 in antibodies (immunoglobulins) (FL-Immuno/36)
Fab, Fc and F(ab')2 in antibodies (immunoglobulins) (FL-Immuno/36)
- Report rights infringement
- published: 10 Jun 2017
- views: 80562
This video lecture explains the origin and significance of terms
Fab
Fc
F(ab')2
We have discussed in brief the key experiments revealing the antibody structure.
9:32
Fc receptors
This video presents the receptors that bind the constant region of antibodies - Fc recepto...
published: 01 Oct 2017
Fc receptors
Fc receptors
- Report rights infringement
- published: 01 Oct 2017
- views: 25858
This video presents the receptors that bind the constant region of antibodies - Fc receptors, including the Fc-gamma receptors and Fc-epsilon receptors.
4:17
Antibody
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produ...
published: 14 Sep 2020
Antibody
Antibody
- Report rights infringement
- published: 14 Sep 2020
- views: 83168
An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region. Each tip of the "Y" of an antibody contains a paratope (analogous to a lock) that is specific for one particular epitope (analogous to a key) on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize its target directly (for example, by inhibiting a part of a microbe that is essential for its invasion and survival). Depending on the antigen, the binding may impede the biological process causing the disease or may activate macrophages to destroy the foreign substance. The ability of an antibody to communicate with the other components of the immune system is mediated via its Fc region (located at the base of the "Y"), which contains a conserved glycosylation site involved in these interactions.[4] The production of antibodies is the main function of the humoral immune system.[5]
Antibodies are secreted by B cells of the adaptive immune system, mostly by differentiated B cells called plasma cells. Antibodies can occur in two physical forms, a soluble form that is secreted from the cell to be free in the blood plasma, and a membrane-bound form that is attached to the surface of a B cell and is referred to as the B-cell receptor (BCR). The BCR is found only on the surface of B cells and facilitates the activation of these cells and their subsequent differentiation into either antibody factories called plasma cells or memory B cells that will survive in the body and remember that same antigen so the B cells can respond faster upon future exposure. In most cases, interaction of the B cell with a T helper cell is necessary to produce full activation of the B cell and, therefore, antibody generation following antigen binding. Soluble antibodies are released into the blood and tissue fluids, as well as many secretions to continue to survey for invading microorganisms.
3:26
Immunology - Antibody Structure & Function
Antibodies, also known as immunoglobulins, are like the ammunition of the body’s humoral d...
published: 24 Jul 2016
Immunology - Antibody Structure & Function
Immunology - Antibody Structure & Function
- Report rights infringement
- published: 24 Jul 2016
- views: 34563
Antibodies, also known as immunoglobulins, are like the ammunition of the body’s humoral defense against microorganisms. Plasma cells are like the turret guns of the immune system that secrete thousands of antibodies per second. You should know the general structure of the 5 types of antibodies, as well as the specific structure of an individual antibody.
First, I’m going to draw a 2 by 2 grid to demonstrate the difference between the light and heavy chains, as well as the variable and constant regions. Each antibody has 2 light chains with a variable region known as V-L and a constant region known as C-L. Each heavy has a variable region known as V-H and three constant regions known as C-H-1, C-H-2, and C-H-3. Disulfide bonds join the light chain to the heavy chain here, and the heavy chains of IgG to each other here. These disulfide bonds bend here at the Hinge region so that the overall antibody structure forms a Y shape.
Four regions, V-L, C-L, V-H, and C-H-1 make up the fragment of antigen binding, or Fab. The variable regions of the Fab fragment determine the specific idiotype: the unique structure of which binds to a corresponding specific antigen. Each B cell expresses only one idiotype of an antibody. As an example, a lab-made immune Fab specific to digoxin is used as an antidote to overdoses of the medication.
C-H-2 and C-H-3 together make up the Fc region of the antibody, which corresponds to the stalk of the Y. C-H-2 has the special property of binding to complement, something I will cover in a future video.
Now let’s discuss the different isotypes of immunoglobulins. There are 5 types: IgG, IgE, IgD, IgM, and IgA. They are differentiated biochemically by their Fc regions and their different functions. All have monomer forms, but only IgA and IgM have different forms when secreted. IgM can exist as a pentamer linked together by disulfide bonds and a J chain, or joining chain. IgA can exist as a dimer with a J chain as well as a Secretory protein. If you were to know just very simple associations to each type then know these. IgM – Immediate response. IgG – delayed response. IgA – mucous membranes. IgE – allergies and parasites. IgD – unclear function.
Question: how many binding sites exist on secreted IgM? Think carefully! Most people’s initial reaction is to say five because secretory IgM exists as a pentamer. However, it is important to remember that each antibody monomer has two binding sites, and thus, secretory IgM has 2 times 5 = 10 binding sites.
Thanks for watching! Be sure to like and subscribe for more.
7:55
تركيب الجسم المضاد (بأختصار)
يشمل هذا المقطع المواضيع التالية:
-Heavy and light chains
-Fab fragment
-Hypervariable reg...
published: 24 Jul 2021
تركيب الجسم المضاد (بأختصار)
تركيب الجسم المضاد (بأختصار)
- Report rights infringement
- published: 24 Jul 2021
- views: 2771
يشمل هذا المقطع المواضيع التالية:
-Heavy and light chains
-Fab fragment
-Hypervariable region
-Fc fragment
0:22
fragment antigen binding region (English) - Medical terminology for medical students -
(Fab region)
A region on an antibody that binds to an antigen.
Cf. complementarity-deter...
published: 26 Jun 2020
fragment antigen binding region (English) - Medical terminology for medical students -
fragment antigen binding region (English) - Medical terminology for medical students -
- Report rights infringement
- published: 26 Jun 2020
- views: 191
(Fab region)
A region on an antibody that binds to an antigen.
Cf. complementarity-determining region
Fragment crystallizable region
The fragment crystallizable region (Fc region) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system. In IgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (CH domains 2–4) in each polypeptide chain. The Fc regions of IgGs bear a highly conserved N-glycosylation site.Glycosylation of the Fc fragment is essential for Fc receptor-mediated activity. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6 linked sialic acid residues.
The other part of an antibody, called the Fab region, contains variable sections that define the specific target that the antibody can bind. By contrast, the Fc region of all antibodies in a class are the same for each species; they are constant rather than variable. The Fc region is, therefore, sometimes incorrectly termed the "fragment constant region".
This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Fragment_crystallizable_region
fragment crystallizable region (English) - Medical...
Antibodies: Structures, types and functions...
Fab, Fc and F(ab')2 in antibodies (immunoglobulins...
Fc receptors...
Antibody...
Immunology - Antibody Structure & Function...
تركيب الجسم المضاد (بأختصار)...