Interaction of δ-Chymotrypsin with Proflavine

Author:

Chen Wendy,Russo Salvatore F.

Abstract

A 1:1 molar stoichiometry has been found for the noncovalent bonding of proflavine with δ-chymotrypsin. The dissociation constant at pH 7.6 is 0.025 mM which is similar to that found by Glazer for the reaction of proflavine with α-chymotrypsin. The difference spectrum produced by the proflavine–δ-chymotrypsin interaction has been studied as a function of pH. It would appear that a group with pK of approximately 6.5 is involved.

Publisher

Canadian Science Publishing

Subject

General Medicine

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. Interaction of 9-Peptidylaminoacridines with Proteins and Nucleic Acids;Journal of Biological Chemistry;1974-01

2. Chymotrypsin;CRC Critical Reviews in Biochemistry;1973-01

3. Acridine dyes as effectors in papain catalysis;Archives of Biochemistry and Biophysics;1972-11

4. The Elusive Permeability Barriers and Binding Sites for Proflavine in Escherichia coli;Antimicrobial Agents and Chemotherapy;1972-06

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