Heterogeneity of Pepsin-Solubilized Human Glomerular Basement Membrane Collagen

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Abstract
The collagen component of isolated glomerular basement membrane was solubilized by limited pepsin digestion and further purified. The amino acid and carbohydrate composition of the final material was very similar to that described for the .alpha.1-chains of type IV collagen. However, the presence of several components was detected when the material was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis without or after reduction. The MW of major components in the reduced material were about 140,000, 100,000, 80,000 and less than 65,000 (in the case of 5 components). However, part of the heterogeneity may be due to the presence of more than 1 collagenous part in a procollagen-type polypeptide chain, and an additional reason may lie in a partial degradation of collagenous portions during pepsin digestion.