Sulfhydryl content of bovine eye lens leucine aminopeptidase. Determination of the reactivity of the sulfhydryl groups of the zinc metalloenzyme, of the enzyme activated by Mg2+, Mn2+, and Co2+, and of the metal-free apoenzyme.-Reference-Cited by-同舟云学术

Sulfhydryl content of bovine eye lens leucine aminopeptidase. Determination of the reactivity of the sulfhydryl groups of the zinc metalloenzyme, of the enzyme activated by Mg2+, Mn2+, and Co2+, and of the metal-free apoenzyme.

Published:1982-06 Issue:12 Volume:257 Page:7086-7091
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cuypers H T,van Loon-Klaassen L A,Egberts W T,de Jong W W,Bloemendal H

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference18 articles.

1. Leucine Aminopeptidase (Bovine Lens)

2. Leucine Aminopeptidase (Bovine Lens)

3. Leucine aminopeptidase (bovine lens). Effect of pH on the relative binding of Zn2+ and Mg2+ to and on activation of the enzyme.

4. Leucine aminopeptidase (bovine lens). The relative binding of cobalt and zinc to leucine aminopeptidase and the effect of cobalt substitution on specific activity.

5. [42] Crystalline leucine aminopeptidase from lens (α-aminoacyl-peptide hydrolase; EC 3.4.11.1)

Cited by 10 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Functional characterization and specific effects of various peptides on enzymatic activity of a DPP-III homologue from goat brain;Journal of Enzyme Inhibition and Medicinal Chemistry;2008-01-01

2. Structure and Mechanism of Bovine Lens Leucine Aminopeptidase;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22

3. Human and Rat Dipeptidyl Peptidase III: Biochemical and Mass Spectrometric Arguments for Similarities and Differences;Biological Chemistry;2000-01-18

4. Nature and regulation of pistil-expressed genes in tomato;Plant Molecular Biology;1995-07

5. Leucine aminopeptidase from Arabidopsis thaliana. Molecular evidence for a phylogenetically conserved enzyme of protein turnover in higher plants;European Journal of Biochemistry;1992-04