Interaction of beta-Amylase with Substrates and Inhibitors with Comments on Koshland's Induced-Fit Theory. A Reply-Reference-Cited by-同舟云学术

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Interaction of beta-Amylase with Substrates and Inhibitors with Comments on Koshland's Induced-Fit Theory. A Reply

Published:1974-05 Issue:1 Volume:44 Page:139-142
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Thoma John A.

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1974.tb03466.x/fullpdf

Reference15 articles.

1. On the Interaction of beta-Amylase with Substrate and Inhibitors, with Comments on Koshland's Induced-Fit Hypothesis

2. Competitive Inhibition by Substrate during Enzyme Action. Evidence for the Induced-fit Theory1,2

3. 3. J. A. Thoma, J. E. Spradlin, S. Dygert, and P. Boyer (1971 ) inThe Enzymes () vol. 5 , third ed. , pp.115 -182 , Academic Press, New York.

4. Die Wirkungsweise von β-Amylase auf Stärkeoligosaccharide

5. Kinetische untersuchungen an β-amylase und phosphorylase. Abhängigkeit der reaktionsgeschwindigkeit von der kettenlänge der amylosen

Cited by 2 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. Affinity Purification of β-Amylases Originating from Plant Using Cyclomaltohexaose-Immobilized Sepharose 6B in the Presence of Ammonium Sulfate;Protein Expression and Purification;1993-08

2. Cycloheptaamylose as an affinity ligand of cereal alpha amylase. Characteristics and a possible mechanism of the interaction;Carbohydrate Research;1982-10

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