Abstract
Two amylase components were purified from human pancreatic juice and investigated for their proteochemical, immunological and enzymatic properties. The two components were similar in molecular weight, amino acid composition and immunoreactivity as determined by radioimmunoassay for the major component of pancreatic amylase. Their specific activity, optimal pH value, and stability were identical. Both were equally activated by chloride ion and their hydrolysis modes of various substrates were also identical. The only difference found between them was in the electrophoretic mobility in the peptide map, indicating that the difference was brought about by deamidation. The quantitative analysis of pancreatic amylase isozymes can provide information on the posttranslational modification in pancreatic tissue and/or in body fluids.
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