V region - translation to Αγγλικά
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V region - translation to Αγγλικά

IMMUNE SYSTEM PROTEIN
Immunoglobulin; Antibodies; Immunoglobulins; Immunoglobulin variable region; Gamma-chain immunoglobulin; Mu-chain immunoglobulin; Immunoglobulin (Ig); Anitbody; Antibody repertoire; Immunoglobuline; Surface immunoglobulin; Fab immunoglobulin; Fc immunoglobulin; Receptors, ige; Receptors, igg; Binding sites, antibody; Variable region; Constant region; Immunoglobin; Receptors, antigen, b-cell; Anti body; Anti-body; Immunoglobulin joining region; Functional antibody; Immunoglobulin structure; Immunoglobulin gene; Immune globulin; Fv Fragments; Immunogloblin; C region; V region; Natural antibody; Natural antibodies; Fragment variable; Fv region; Variable fragment; Constant domain; Variable domain; Theories of antibody; Civacir; Anti-bodies; Polyvalent antibody; Polyvalent antibodies; Monovalent antibody; Monovalent antibodies; Specific antibody; Unspecific antibodies; Unspecific antibody; Specific antibodies; Immunoglobulin diversity; Immunologlobulins; IgG IgM; Antibody response; Binding Antibody Unit; Binding antibody unit; Binding antibody units; BAU/mL; BAU (unit); IgM pentamer; IgM hexamer; IgM tetramer
  • access-date=12 December 2008}}</ref>
  • Each antibody binds to a specific [[antigen]]; an interaction similar to a lock and key.
  •  Phagocytosis occurs as the pathogen is ingested.
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  • Schematic structure of an antibody: two heavy chains (blue, yellow) and the two light chains (green, pink). The antigen binding site is circled.
  • Mechanism of class switch recombination that allows isotype switching in activated B cells
  • 1IGT}})
  • FITC]].
  • The secreted mammalian [[IgM]] has five Ig units. Each Ig unit (labeled 1) has two epitope binding [[Fab region]]s, so IgM is capable of binding up to 10 epitopes.
  • [[Michael Heidelberger]]
  • complexes]] that bind to multiple antigen molecules.
  • Simplified overview of V(D)J recombination of immunoglobulin heavy chains

V region         

общая лексика

вариабельная область

V-область

V-домен

V-сегмент (иммуноглобулина)

синоним

variable region

v.         
NOVEL BY THOMAS PYNCHON
V., A Novel; V. (novel)
v. I verse noun стих; стихотворная строка II vide noun lat. смотри, см.
v.         
NOVEL BY THOMAS PYNCHON
V., A Novel; V. (novel)

существительное

общая лексика

стих

стихотворная строка

Латинский язык

смотри, см.

синоним

verse; vide

Ορισμός

УЛАФ V
(Olav V) (1903-1991), король Норвегии, родился 2 июля 1903 в Англии, сын принца Карла Датского и принцессы Мод Английской. После расторжения в 1905 унии между Швецией и Норвегией, Александра перевезли в Норвегию, где дали новое норвежское имя - Улаф. С ранних лет Улаф получал приличествующее наследнику трона образование. В 18-летнем возрасте стал посещать заседания кабинета министров и осуществлять функции монарха. Учился в университете Осло и Норвежской военной академии, затем в Бейллиол-колледже Оксфордского университета. В 1929 женился на принцессе Марте Шведской.
В годы Второй мировой войны, после оккупации Норвегии, Улаф находился в эмиграции в Англии. В июле 1944 он стал командующим вооруженными силами Норвегии. В мае 1945 после победы над нацистами Улаф первым из представителей королевской семьи вернулся в Норвегию. С июня 1955 до смерти отца 21 сентября 1957 был регентом. 20 января 1958 при открытии заседания парламента Улаф присягнул на верность Норвегии как король Улаф V. Умер Улаф 17 января 1991.

Βικιπαίδεια

Antibody

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen. 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 it directly (for example, by blocking a part of a virus that is essential for its invasion).

To allow the immune system to recognize millions of different antigens, the antigen-binding sites at both tips of the antibody come in an equally wide variety. In contrast, the remainder of the antibody is relatively constant. It only occurs in a few variants, which define the antibody's class or isotype: IgA, IgD, IgE, IgG, and IgM. The constant region at the trunk of the antibody includes sites involved in interactions with other components of the immune system. The class hence determines the function triggered by an antibody after binding to an antigen, in addition to some structural features. Antibodies from different classes also differ in where they are released in the body and at what stage of an immune response.

Together with B and T cells, antibodies comprise the most important part of the adaptive immune system. They occur in two forms: one that is attached to a B cell, and the other, a soluble form, that is unattached and found in extracellular fluids such as blood plasma. Initially, all antibodies are of the first form, attached to the surface of a B cell – these are then referred to as B-cell receptors (BCR). After an antigen binds to a BCR, the B cell activates to proliferate and differentiate into either plasma cells, which secrete soluble antibodies with the same paratope, or memory B cells, which survive in the body to enable long-lasting immunity to the antigen. Soluble antibodies are released into the blood and tissue fluids, as well as many secretions. Because these fluids were traditionally known as humors, antibody-mediated immunity is sometimes known as, or considered a part of, humoral immunity. The soluble Y-shaped units can occur individually as monomers, or in complexes of two to five units.

Antibodies are glycoproteins belonging to the immunoglobulin superfamily. The terms antibody and immunoglobulin are often used interchangeably, though the term 'antibody' is sometimes reserved for the secreted, soluble form, i.e. excluding B-cell receptors.

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