Calorimetric investigations of the binding of inhibitors to α-chymotrypsin. I. Enthalpy of dilution of α-chymotrypsin and of proflavine, and the enthalpy of binding of indole, N-acetyl-D-tryptophan, and proflavine to α-chymotrypsin-Reference-Cited by-同舟云学术

Calorimetric investigations of the binding of inhibitors to α-chymotrypsin. I. Enthalpy of dilution of α-chymotrypsin and of proflavine, and the enthalpy of binding of indole, N-acetyl-D-tryptophan, and proflavine to α-chymotrypsin

Published:1969-12-01 Issue:12 Volume:8 Page:4910-4917
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Shiao Daniel D. F.,Sturtevant Julian M.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00840a039

Reference36 articles.

1. On the interaction of the active site of α-chymotrypsin with chromophores: Proflavin binding and enzyme conformation during catalysis

2. Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

3. MICROCALORIMETRIC AND KINETIC STUDIES OF THE α-CHYMOTRYPSIN – HYDROCINNAMIC ESTER – HYDROCINNAMIC ACID SYSTEM

4. Ultraviolet spectral changes related to the enzymic activity of chymotrypsin

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