Who proposed the basic structure of immunoglobulin? How many polypeptide chains are present in it.
Answers
Answer:
Gerald Edelman
It has four polypeptide chains
Explanation:
In the 1920s, Michael Heidelberger and Oswald Avery observed that antigens could be precipitated by antibodies and went on to show that antibodies are made of protein.[19] The biochemical properties of antigen-antibody-binding interactions were examined in more detail in the late 1930s by John Marrack.
A major advance in these structural studies was the discovery in the early 1960s by Gerald Edelman and Joseph Gally of the antibody light chain,[23] and their realization that this protein is the same as the Bence-Jones protein described in 1845 by Henry Bence Jones.[24] Edelman went on to discover that antibodies are composed of disulfide bond-linked heavy and light chains.
Two identical heavy chains (H) and two identical light chains (L).
The amino terminal ends of the polypeptide chains show considerable variation in amino acid composition and are referred to as the variable (V) regions to distinguish them from the relatively constant (C) regions. Each L chain consists of one variable domain, VL, and one constant domain, CL. The H chains consist of a variable domain, VH, and three constant domains CH1, CH2 and CH3. Each heavy chain has about twice the number of amino acids and molecular weight (~50,000) as each light chain (~25,000), resulting in a total immunoglobulin monomer molecular weight of approximately 150,000.