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- W1964374155 abstract "Properties of carboxypeptidase A of cultured skin fibroblasts from control and cystic fibrosis patients were studied using α-N-carbobenzoxy-l-glutamyl-l-tyrosine as substrate. Carboxypeptidase A was inhibited by thiomersal, cyanide, iodoacetate and N-ethylmaleimide in a similar manner for control and cystic fibrosis fibroblasts. Both trypsin and dithiothreitol treatment activated the enzyme, but 1,10-phenanthroline inhibited only in the presence of dithiothreitol. Both Zn2+ and Co2+ reversed this inhibition. Trypsin treatment of carboxypeptidase A produced a form of the enzyme having a higher km value for both control and cystic fibrosis fibroblasts. Dithiothreitol treatment of control fibroblasts resulted in a form with similar properties to the trypsin activated form, but cystic fibrosis fibroblasts yielded a variant form with even higher km and Vmax values. Since other properties were similar, it seems likely that this difference reflected binding of a molecule to the enzyme rather than of a defect in the enzyme." @default.
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- W1964374155 date "1978-07-01" @default.
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- W1964374155 title "Carboxypeptidase A activity of cultured skin fibroblasts and relationship to cystic fibrosis" @default.
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- W1964374155 doi "https://doi.org/10.1016/0009-8981(78)90058-x" @default.
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