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Extra resources for The Plasma Proteins. Structure, Function, and Genetic Control
Example text
This is illustrated in Fig. 5, which s h o w s the location of the oligosaccharides in h u m an I g M, IgA, and IgG.
1974) and M e n d ez et al. , to Cys-47 1 in the s e q u e n ce of the h u m an al chain s h o w n in Section V I , D . T he J chain a p p e a rs t o b e b o u nd t o t he h o m o l o g o us C-terminal cysteine in the ì chain (Cys-575 ) but only to o ne or t w o of the ten ì chains (Sections V I , C and V I I I , B ). T he precise role of J chain in polymerization of IgA and IgM and its function in the final structure of the p o l y m e r s are still u n s o l v e d. fî. The Heavy-Chain Constant 1.
Tryptic cleavage of IgM at 60°C give s good yield s of F ab and a p e n t a m e r ic ( F c ^ )5 , b ut t he second c o n s t a nt domain (C M2) is excised and degraded to peptides. A t 37°C the yield s wit h trypsin are p o o r, and the fragments vary wit h time and are poorly characterized. O t h er e n z y m e s such as plasmin m ay r e m o v e the C-terminal d o m a in of s o m e immunoglobulins. Occasionally, proteolytic cleavage of m y e l o m a globulins p r o d u c es Fv fragments, which r e p r e s e nt noncovalent associations of the V L and V H regions.
