دورية أكاديمية
Purification and characterization of two Cl- -activated aminopeptidases hydrolysing basic termini from human skeletal muscle.
العنوان: | Purification and characterization of two Cl- -activated aminopeptidases hydrolysing basic termini from human skeletal muscle. |
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المؤلفون: | Mantle, David, Lauffart, Brenda, McDermott, John R., Kidd, Alison M., Pennington, J. T. |
المصدر: | European Journal of Biochemistry; 3/1/85, Vol. 147 Issue 2, p307-312, 6p |
مصطلحات موضوعية: | CHLORINE, AMINOPEPTIDASES, HUMAN skeleton, MUSCLES, PEPTIDES, AMINO acids |
مستخلص: | Two aminopeptidases (I and II), hydrolysing basic termini, were purified to homogeneity (as judged by polyacrylamide gel electrophoresis) from human. quadriceps muscle by anion-exchange chromatography and preparative electrophoresis. The electrophoretic migration rate of II was approximately 80% of that of I. Both enzymes had the following properties: optimum activity was at pH 6.5; addition of 0.15 M Cl- or Br- anions resulted in 20-fold or 10-fold increase inactivity respectively. There was little or no increase in activity on the addition of other anions, or divalent cations (0.5 - mM). Approximately 50% inhibition of activity was obtained in the presence of bestatin (0.1μM), p-hydroxymercuriphenylsuphonic acid (0.1μM) EDTA (10 mM) 1,10-phenanthroline (100 &muM), N-ethylmalimide (1mM) and BuI-Thr-Phe-Pro (0.5mM). The molecular mass was 72000 Da (gel filtration). Only the arginyl and lysyl 7-amino-4-methylcoumarin (Amc) derivatives wer appreciablyhydrolysed; approximate K |
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قاعدة البيانات: | Complementary Index |
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