Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa

Author:

Doumeng C,Maroux S

Abstract

Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa, was purified to homogeneity. The pure enzyme is a glycoprotein containing a very small amount of sugar. It is composed of only one subunit of 50,000 mol. wt. and possesses 1 zinc atom per molecule. Its specificity is primarily directed towards tripeptides with an N-terminal proline residue. However, the enzyme is also able to hydrolyse other tripeptides, except those with either a charged amino acid in the N-terminal position or a proline residue in the second position. The purified aminotripeptidase accounts for almost all the tripeptidase activity of the soluble fraction from intestinal mucosa.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

Cited by 28 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. Tripeptide Aminopeptidase;Handbook of Proteolytic Enzymes;2013

2. Digestion and Absorption of Nutrients and Vitamins;Sleisenger and Fordtran's Gastrointestinal and Liver Disease;2010

3. Studies on Transport of Amino Acids from Peptides by Rat Small Intestine in vitro;European Journal of Biochemistry;2005-03-03

4. Tripeptide aminopeptidase;Handbook of Proteolytic Enzymes;2004

5. Modification of Leukotriene A4 Hydrolase/Aminopeptidase by Sulfhydryl-Blocking Reagents: Differential Effects on Dual Enzyme Activities by Methyl-Methane Thiosulfonate;Archives of Biochemistry and Biophysics;1999-08

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