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Calorimetric investigations of the binding of inhibitors to alpha-chymotrypsin. I. The enthalpy of dilution of alpha-chymotrypsin and of proflavin, and the enthalpy of binding of indole, N-acetyl-D-tryptophan, and proflavin to alpha-chymotrypsin.

作者信息

Shiao D D, Sturtevant J M

出版信息

Biochemistry. 1969 Dec;8(12):4910-7. doi: 10.1021/bi00840a039.

DOI:10.1021/bi00840a039
PMID:5391863
Abstract
摘要

相似文献

1
Calorimetric investigations of the binding of inhibitors to alpha-chymotrypsin. I. The enthalpy of dilution of alpha-chymotrypsin and of proflavin, and the enthalpy of binding of indole, N-acetyl-D-tryptophan, and proflavin to alpha-chymotrypsin.
Biochemistry. 1969 Dec;8(12):4910-7. doi: 10.1021/bi00840a039.
2
Calorimetric investigations of the binding of inhibitors to alpha-chymotrypsin. II. A systematic comparison of the thermodynamic functions of binding of a variety of inhibitors to alpha-chymotrypsin.
Biochemistry. 1970 Mar 3;9(5):1083-90. doi: 10.1021/bi00807a005.
3
A calorimetric investigation of the binding of indole and phenylethane boronic acid to chymotrypsin.
J Biol Chem. 1983 Feb 25;258(4):2135-42.
4
Binding properties of oligomeric alpha-chymotrypsin.寡聚α-胰凝乳蛋白酶的结合特性
Biochemistry. 1971 Mar 16;10(6):1033-41. doi: 10.1021/bi00782a015.
5
Light and ultrasonic regulation of alpha-chymotrypsin catalytic activity. Proflavin as a light- and sound-sensitive competitive inhibitor.α-糜蛋白酶催化活性的光和超声调节。原黄素作为一种对光和声音敏感的竞争性抑制剂。
FEBS Lett. 1974 Mar 1;39(3):329-31. doi: 10.1016/0014-5793(74)80142-0.
6
Thermodynamics of binding to native alpha-chymotrypsin and to forms of alpha-chymotrypsin in which catalytically essential residues are modified; a study of "productive" and "nonproductive" associations.与天然α-胰凝乳蛋白酶以及催化必需残基被修饰的α-胰凝乳蛋白酶形式的结合热力学；对“有效”和“无效”缔合的研究。
Biochemistry. 1977 May 17;16(10):2194-202. doi: 10.1021/bi00629a024.
7
Inactivation of alpha-chymotrypsin by a bifunctional reagent, 2-bromomethyl-3, I-benzoxazin-4-one.
Biochim Biophys Acta. 1973 Jun 6;309(2):379-96. doi: 10.1016/0005-2744(73)90037-5.
8
Interactions of alpha-chymotrypsin with peptides containing tryptophan or its derivatives at the C-terminus.α-胰凝乳蛋白酶与C末端含色氨酸或其衍生物的肽的相互作用。
J Biochem. 1977 Jul;82(1):231-7. doi: 10.1093/oxfordjournals.jbchem.a131674.
9
Structure of crystalline alpha-chymotrypsin. 3. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin.结晶α-胰凝乳蛋白酶的结构。3. 与α-胰凝乳蛋白酶活性位点结合的底物和抑制剂的晶体学研究。
J Mol Biol. 1969 Dec 14;46(2):337-48. doi: 10.1016/0022-2836(69)90426-4.
10
Kinetics of the interaction of bovine pancreatic trypsin inhibitor (Kunitz) with alpha-chymotrypsin.牛胰蛋白酶抑制剂（库尼兹）与α-糜蛋白酶相互作用的动力学
Biochemistry. 1974 Jun 4;13(12):2512-20. doi: 10.1021/bi00709a600.

引用本文的文献

1
Protonation linked equilibria and apparent affinity constants: the thermodynamic profile of the alpha-chymotrypsin-proflavin interaction.质子化相关平衡与表观亲和常数：α-糜蛋白酶-原黄素相互作用的热力学概况
Eur Biophys J. 2007 Dec;37(1):11-8. doi: 10.1007/s00249-007-0148-0. Epub 2007 Apr 19.
2
Self-association of alpha-chymotrypsin at low ionic strength in the vicinity of its pH optimum.在最适pH值附近的低离子强度条件下α-糜蛋白酶的自缔合作用。
Biochem J. 1977 Mar 1;161(3):687-94. doi: 10.1042/bj1610687.