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Characterization of two thiol-dependent aminopeptidases partially purified from human placenta.

作者信息

Lampelo S, Lalu K, Vanha-Perttula T

出版信息

Int J Biochem. 1983;15(5):709-14. doi: 10.1016/0020-711x(83)90196-9.

Abstract
  1. Two thiol-dependent aminopeptidases (I and III) were partially purified from the soluble fraction of human placenta. 2. Aminopeptidase I preferred L-alanine-beta-naphthylamide (AlaNA) as substrate at pH 7.0-7.5. It was sensitive to heat and some divalent metal ions (Co2+, Ni2+, Zn2+) but resistant to EDTA, and some amino acids. 3. Aminopeptidase III hydrolysed equally well AlaNA and ArgNA at pH 6.5-7.0. It was markedly suppressed by EDTA and reactivated by Co2+. It was inhibited by heat, some amino acids, benzamadine and puromycin.
摘要

相似文献

1
Characterization of two thiol-dependent aminopeptidases partially purified from human placenta.
Int J Biochem. 1983;15(5):709-14. doi: 10.1016/0020-711x(83)90196-9.
3
Characterization of three aminopeptidases purified from maternal serum.
Biochim Biophys Acta. 1986 Sep 26;873(2):190-7. doi: 10.1016/0167-4838(86)90045-2.

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