Immunoglobulin (English Version)

Immunoglobulin (Ig) is a protein secreted by plasma cells, the differentiated B cells, and binds with a particular antigen. Immunoglobulin is also called antibody. All antibodies have the same Y-shaped structure and in their monomer form consists of two identical heavy chains and two identical light chains.¹ Immunoglobulin is divided by five classes, namely IgG, IgM, IgA, IgD and IgE.² Those classes are determined by the structure difference in heavy-chain constant region. For this reason, those classes have no effects towards the antibody specifity, whereas the antibody specifity is determined by antigen binding sites.³

Immunoglobulins belong to the group of glycoproteins called globulins. Immunoglobulin consists of four polypeptides chains, that is two identical Heavy (H) chains and two identical Light (L) chains. In every H and L chain are two distinct regions. In the tips of the chain, there is V (variable) region as the sites of antigen binding. It is V region that recognizes and attaches specifically to particular antigen.³ The remainder L and H is the constant (C) region, nearly the same to all antibodies in the same class, is responsible on the kind of antigen-antibody reactions occurs.²

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Immunoglobulin

Immunoglobulin (Ig) adalah suatu protein yang disekresikan oleh sel-sel plasma, yaitu sel-sel B yang terdiferensiasi, dan berikatan dengan suatu antigen tertentu. Immunoglobulin juga disebut dengan antibodi. Semua antibodi memiliki struktur berbentuk Y yang sama dan dalam bentuk monomernya terdiri atas dua rantai berat identik dan dua rantai ringan identik.¹ Immunoglobulin dibagi menjadi lima kelas, yaitu IgG, IgM, IgA, IgD, dan IgE.² Kelas-kelas tersebut ditentukan berdasarkan perbedaan struktur pada segmen konstanta rantai-berat. Untuk alasan inilah, kelas-kelas tersebut tidak memiliki efek pada ke-spesifik-an antibodi tersebut, dimana kekhususan antibodi ditentukan oleh tempat ikat antigen.³

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