一个电离基团在控制胰凝乳蛋白酶构象和活性中的作用 - Suppr

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超能文献

Implication of an ionizing group in the control of conformation and activity of chymotrypsin.

作者信息

Oppenheimer H L, Labouesse B, Hess G P

出版信息

J Biol Chem. 1966 Jun 10;241(11):2720-30.

PMID:5911643

Abstract

摘要

相似文献

Implication of an ionizing group in the control of conformation and activity of chymotrypsin.一个电离基团在控制胰凝乳蛋白酶构象和活性中的作用

J Biol Chem. 1966 Jun 10;241(11):2720-30.

Physico-chemical characterization of tyrosyl residues in alpha-chymotrypsinogen and pi-chymotrypsin.α-胰凝乳蛋白酶原和π-胰凝乳蛋白酶中酪氨酸残基的物理化学特性

J Biochem. 1965 Jul;58(1):60-7. doi: 10.1093/oxfordjournals.jbchem.a128165.

Formaldehyde as an active site label of -chymotrypsin.甲醛作为α-胰凝乳蛋白酶的活性部位标记物。

Can J Biochem. 1972 Oct;50(10):1114-21. doi: 10.1139/o72-152.

Modification of the amino group of isoleucine-16 in chymotrypsin with retention of activity.在保留活性的情况下对胰凝乳蛋白酶中异亮氨酸-16的氨基进行修饰。

Biochem Biophys Res Commun. 1971 May 7;43(3):510-5. doi: 10.1016/0006-291x(71)90643-7.

Studies on chymotrypsin-P. II. Kinetics.

Can J Biochem. 1972 Jul;50(7):846-7. doi: 10.1139/o72-119.

Thermal perturbation difference spectra of proteins containing tryptophyl residues.含色氨酸残基蛋白质的热扰动差光谱。

Biochemistry. 1970 Sep 1;9(18):3562-8. doi: 10.1021/bi00820a009.

Conformational changes accompanying the formation of chymotrypsin-substrate complexes. Evidence for the involvement of an N-terminal alpha-amino group in the activity and the conformation of the enzyme.

Biochem Biophys Res Commun. 1964;14:318-22. doi: 10.1016/s0006-291x(64)80003-6.

Study of the polarity of the active site of chymotrypsin.胰凝乳蛋白酶活性位点的极性研究。

Biochemistry. 1966 Jun;5(6):1979-83. doi: 10.1021/bi00870a027.

pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method.胰凝乳蛋白酶催化作用的pH依赖性。附录：通过X射线衍射和平衡法研究底物与二聚体α-胰凝乳蛋白酶的结合

Biochemistry. 1974 Mar 26;13(7):1416-26. doi: 10.1021/bi00704a016.

Interaction of actinomycin D with the chymotrypsinogen-DNA complex.放线菌素D与胰凝乳蛋白酶原-DNA复合物的相互作用。

Biochim Biophys Acta. 1968 Dec 17;169(2):457-65. doi: 10.1016/0005-2787(68)90054-3.

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Loop dynamics of the extracellular domain of human tissue factor and activation of factor VIIa.人组织因子细胞外结构域的环动力学与凝血因子VIIa的激活

Biophys J. 2009 Jan;96(2):681-92. doi: 10.1016/j.bpj.2008.10.018.

Specificity and stereospecificity of alpha-chymotrypsin.α-胰凝乳蛋白酶的特异性和立体特异性

Biochem J. 1967 Aug;104(2):369-77. doi: 10.1042/bj1040369.

The binding of inhibitors to alpha-chymotrypsin at alkaline pH.在碱性pH条件下抑制剂与α-糜蛋白酶的结合。

Biochem J. 1967 May;103(2):428-30. doi: 10.1042/bj1030428.

Optical and chemical identification of kinetic steps in trypsin- and chymotrypsin-catalysed reactions.胰蛋白酶和胰凝乳蛋白酶催化反应中动力学步骤的光学与化学鉴定。

Biochem J. 1966 Nov;101(2):411-6. doi: 10.1042/bj1010411.

Reaction of acetyl-alpha-chymotrypsin and other esters with an ionizable nucleophile, monoisonitrosoacetone.乙酰-α-胰凝乳蛋白酶及其他酯类与可电离亲核试剂单异亚硝基丙酮的反应

Proc Natl Acad Sci U S A. 1970 Apr;65(4):1120-6. doi: 10.1073/pnas.65.4.1120.

Alkaline pH dependence of delta-chymotrypsin-catalyzed hydrolysis of specific substrates.δ-胰凝乳蛋白酶催化特定底物水解的碱性pH依赖性

Proc Natl Acad Sci U S A. 1969 Aug;63(4):1214-21. doi: 10.1073/pnas.63.4.1214.

Pi-, delta-, and gamma-chymotrypsin: three-dimensional electron-density and difference maps at 5 A resolution, and comparison with chymotrypsinogen.π-、δ-和γ-胰凝乳蛋白酶：5埃分辨率下的三维电子密度图和差值图，以及与胰凝乳蛋白酶原的比较。

Proc Natl Acad Sci U S A. 1967 Jul;58(1):304-11. doi: 10.1073/pnas.58.1.304.

The alkaline pH dependence of chymotrypsin reactions: postulation of a pH-dependent intramolecular competitive inhibition.胰凝乳蛋白酶反应的碱性pH依赖性：pH依赖性分子内竞争性抑制的假设

Proc Natl Acad Sci U S A. 1966 Sep;56(3):833-9. doi: 10.1073/pnas.56.3.833.

Inactivation of chymotrypsin by diphenyldiazomethane.二苯基重氮甲烷对胰凝乳蛋白酶的失活作用。

Proc Natl Acad Sci U S A. 1966 Oct;56(4):1252-9. doi: 10.1073/pnas.56.4.1252.

Competitive labelling, a method for determining the reactivity of individual groups in proteins. The amino groups of porcine elastase.竞争性标记，一种确定蛋白质中各个基团反应性的方法。猪弹性蛋白酶的氨基。

Biochem J. 1971 Sep;124(2):289-99. doi: 10.1042/bj1240289.

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