Leucine Aminopeptidase (Bovine Lens)
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چکیده
The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,000 f 4000 in the presence or absence of mercaptoethanol. A similar value (57,000) for the subunit of the enzyme or its carboxamidomethylated derivative was found on gel electrophoresis after incubation in 0.1 to 1.2 % sodium dodecyl sulfate in the presence of mercaptoethanol.
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Leucine Aminopeptidase (Bovine Lens)
The stability to pH and denaturing agents of crystalline leutine aminopeptidase (bovine lens) (EC 3.4.1.1) is reported. The native enzyme exhibited a molecular weight of 327,000. In 7 M urea below pH 3 and in 23.7 M guanidinium chloride below pH 8.5, both leucine aminopeptidase and its reduced and carboxamidomethylated derivative exhibited a molecular weight on equilibrium centrifugation of 54,...
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Rabbit antisera to purified bovine lens leucine aminopeptidase (EC 3.4.11.1, LAP) were prepared and shown to be specific for leucine aminopeptidase alone (Taylor et al Cur Eye Res 2:47-56, 1982). When whole hog lens thin sections were treated first with these antisera and then with fluorescein conjugated goat anti-rabbit gamma globulin, greatest fluorescence was observed in the elongating epith...
متن کاملLeucine Aminopeptidase (Bovine Lens)
Spark emission and atomic absorption spectroscopy of crystalline leucine aminopeptidase (bovine lens) (EC 3.4.1.1) shows the presence of 2 zinc atoms per subunit molecular weight of 54,000 (12 zinc atoms per oligomer of 320,000). Removal of zinc by dialysis yields a zinc-free product with no enzymatic activity which upon readdition of Zn2+, regains full activity with the concomitant binding of ...
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The zinc-dependent leucine aminopeptidase from Pseudomonas putida (ppLAP) is an important enzyme for the industrial production of enantiomerically pure amino acids. To provide a better understanding of its structure-function relationships, the enzyme was studied by X-ray crystallography. Crystal structures of native ppLAP at pH 9.5 and pH 5.2, and in complex with the inhibitor bestatin, show th...
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