Biosynthesis of membrane bound Ig and secretion of Ig by chicken lymphoid cells.
The metabolic turnover of membrane proteins of chicken lymphoid cells is studied, using a double isotope labeling technique (i.e., [14C]amino acid pulse and [3H]leucine chase). Compared with other membrane proteins, the metabolic turnover of membrane bound immunoglobulins (M-Ig) is very slow. There was no difference in the turnover between M-Ig and specific antigen binding receptor immunoglobulins. Immunoglobulins appear to be a stable constituent of the lumphocyte membrane. Cellular kinetic experiments show that the rate of biosynthesis of secreted immunoglobulins (S-Ig) is nearly ten times as much as that of M-Ig, suggesting that metabolic pathway leading to M-Ig are distinct from those leading to S-Ig. The difference in 3H/14C ratios between S-Ig and M-Ig reflects the rate of biosynthesis of these immunoglobulins by two types of bursa derived lymphoid cells.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D002645:Chickens; D007136:Immunoglobulins / Q000096:biosynthesis* / Q000378:metabolism; D007930:Leucine / Q000378:metabolism; D008214:Lymphocytes / Q000378:metabolism*; D008297:Male; D014176:Protein Biosynthesis
D000596:Amino Acids; D007136:Immunoglobulins; D007930:Leucine