3,4,5,6-tetrahydrophthalic anhydride modification of glutamate dehydrogenase: The construction and activity of heterohexamers-Reference-Cited by-同舟云学术

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3,4,5,6-tetrahydrophthalic anhydride modification of glutamate dehydrogenase: The construction and activity of heterohexamers

Published:1988-06 Issue:2 Volume:263 Page:315-322
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

O'Connell Lisa I.,Bell Evelyn T.,Bell J.Ellis

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference18 articles.

1. Structural features of tropoelastin related to the sites of cross-links in aortic elastin

2. Studies on the viscosity of solutions of bovine liver glutamate dehydrogenase and on related hydrodynamic models; effect of toluene on enzyme association

3. Catalytic activity of bovine glutamate dehydrogenase requires a hexamer structure

4. Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase

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1. Allosterism and Drug Discovery;Burger's Medicinal Chemistry and Drug Discovery;2021-04-27

2. Allosteric Proteins and Drug Discovery;Burger's Medicinal Chemistry and Drug Discovery;2010-09-15

3. Allosteric Proteins and Drug Discovery;Burger's Medicinal Chemistry and Drug Discovery;2003-01-15

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