Isolation and Purification of Arylamidase from Human Lenses
- 1 January 1974
- journal article
- Published by S. Karger AG in Ophthalmic Research
- Vol. 6 (2-4) , 235-244
- https://doi.org/10.1159/000264708
Abstract
A procedure is described for the resolution of arylamidase from human lenses. Purified arylamidase will hydrolyze leucyl-, arginyl- and lysyl-β-naphtylamides. It has been shown to be ependent on metal ions for activity. Human arylamidase required dithiothreitol for stability; activity was increased by β-mercapto-ethanol and cysteine and inhibited by p-chloromercuribenzoate. The properties of human lens arylamidase is distinct from leucine aminopeptidase (EC 3.4.1.1) or esterases.Keywords
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