Ostrich (Struthio camelus) carboxypeptidase B: Purification, kinetic properties and characterization of the pancreatic enzyme-Reference-Cited by-同舟云学术

Ostrich (Struthio camelus) carboxypeptidase B: Purification, kinetic properties and characterization of the pancreatic enzyme

Published:1996-05 Issue:5 Volume:28 Page:521-529
ISSN:1357-2725
Container-title:The International Journal of Biochemistry & Cell Biology
language:en
Short-container-title:The International Journal of Biochemistry & Cell Biology

Author:

Bradley Graeme,Naudé Ryno J.,Muramoto Koji,Yamauchi Fumio,Oelofsen Willem

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry

Reference50 articles.

1. Affinity chromatography of pancreatic carboxypeptidases using a carboxypeptidase inhibitor from potatoes as ligand;Ager;Anal. Biochem.,1977

2. Ligand bindings of bovine carboxypeptidase B. 1. Kinetic studies using dipeptide substrates and their carboxyl terminal amino acid analogs;Akanuma;J. Biochem.,1979

3. Kinetic properties of carboxypeptidase B in solutions and crystals;Alter;Biochemistry,1977

4. Carboxypeptidase A;Auld,1987

5. Ostrich (Struthio camelus) carboxypeptidase A: purification, kinetic properties and characterization of the pancreatic enzyme;Bradley;Int. J. Biochem.,1994

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