Abstract
For this investigation highly purified brush border membranes from human small intestine, prepared according to the method described in the preceding paper [1], have been used. Solubilisation of brush border membrane proteins by sodium dodecyl sulphate, Triton X-100 and papain followed by electrophoresis in polyacrylamide gels revealed six distinct peptide hydrolases. These included the enzymes aminopeptidase A (EC 3.4.11.7), dipeptidylpeptidase IV (EC 3.4.14.-), gamma-glutamultranspeptidase (EC 2.3.2.2) and aminopeptidase M (EC 3.4.11.2), which were clearly separable on polyacrylamide gels after solubilisation with Triton X-100 or papain. Activity recovered in the aminopeptidase M peak in the above gel system could be resolved into two distinct peptidases in addition to aminopeptidase M, by SDS-gel-electrophoresis. One of these peptidases was most active towards aliphatic tripeptide (aminopeptidase 1) while the other appeared to be specific for dipeptides (aminopeptidase 2).
Published Version
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