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  • Title: Characterization of three aminopeptidases purified from human placenta.
    Author: Lampelo S, Lalu K, Vanha-Perttula T.
    Journal: Placenta; 1983; 4 Spec No():499-513. PubMed ID: 6424106.
    Abstract:
    Three aminopeptidases purified from the human placenta were characterized and compared with each other. Aminopeptidase II1 preferred L-arginine- and L-lysine-beta-naphthylamides or p-nitroanilides as substrate, with low or negligible hydrolysis of other amino acid derivatives. It was inhibited by L-arginine, L-lysine and L-methionine. This enzyme activity was highly sensitive to heat treatment, N-ethylmaleimide, p-chloromercuribenzoate, puromycin, bestatin, epsilon-amino-n-caproic acid (EACA) and EDTA. After EDTA, this enzyme could be reactivated by Co2+. It is concluded that aminopeptidase II1 is identical with arginine aminopeptidase (EC 3.4.11.6) from other mammalian tissues. Aminopeptidase II2 preferred L-alanine-beta-naphthylamide and p-nitroanilide as substrates. It was also able to hydrolyse L-leucine, L-arginine, L-methionine and L-lysine derivatives but only very weakly L-cystine and Bz-L-cysteine substrates. This enzyme was inhibited by L-arginine, L-alanine, L-lysine and most strongly by L-leucine and L-methionine. It was resistant to bestatin and heat treatment but sensitive to EACA. EDTA caused a marked suppression, which could be prevented by Co2+ and Zn2+. These characteristics are reminiscent of those of alanine aminopeptidase (EC 3.4.11.-) found in other tissues. The third enzyme was the only one clearly particle bound and was therefore called PB-aminopeptidase. It preferred L-leucine derivatives as substrate but also readily hydrolysed other amino acid-beta-naphthylamides and p-nitroanilides including L-cystine and Bz-L-cysteine substrates. Among the amino acids L-cysteine, L-leucine and L-methionine were inhibitory. Bestatin and thiol reagents were without effect and EACA was only moderately inhibitory. EDTA caused a strong suppression, which could be prevented by Co2+ and Zn2+. These properties are equal to those previously described for the placental cystine aminopeptidase (oxytocinase) (EC 3.4.11.3). All three enzymes had an optimum close to neutral pH but apparent differences in their Km and Vmax values with various substrates. These findings suggest that the three purified aminopeptidases are distinct enzymes. Two of these (aminopeptidases II1 and II2) have not previously been isolated and characterized in the human placenta.
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