An intermediate in the pH-induced dissociation of glutamate dehydrogenase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference3 articles.
1. The kinetic measurement of the α-β dissociation of glutamate dehydrogenase
2. The role of tyrosyl-hydrogen bonds in the quaternary structure of the glutamate dehydrogenase molecule
3. A kinetic investigation of the interaction of .alpha.-methylaspartic acid with aspartate aminotransferase
Cited by 4 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. Two-step binding of adenosine diphosphate to L-glutamate dehydrogenase. Effect on the binding of reduced nicotinamide adenine diphosphate and on enzymic catalysis;Biochemistry;1974-05
2. Role of zinc in horse liver alcohol dehydrogenase. III. Influence on structure and conformational changes;Biochemistry;1972-03-01
3. Subunit interactions of lobster hemocyanin;Archives of Biochemistry and Biophysics;1971-01
4. L-Glutamate Dehydrogenases* *Research work cited in this review which originates in the author's laboratory was supported in part by research grant AM 13332, United States Public Health Service and research grant GB 26583X from the National Science Foundation.;Current Topics in Cellular Regulation;1971
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