Journal ArticleDOI
Structure and mechanism in the enzymic activity of carboxypeptidase A and relations to chemical sequence
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This article is published in Accounts of Chemical Research.The article was published on 1970-03-01. It has received 126 citations till now. The article focuses on the topics: Carboxypeptidase A & Carboxypeptidase.read more
Citations
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Book ChapterDOI
Physical Organic Model Systems and the Problem of Enzymatic Catalysis
TL;DR: Rate enhancements have been obtained in several simple chemical reactions that are of similar magnitude to those observed in analogous enzyme-catalyzed reactions, and the goal of analyzing the individual factors that can give such large rate accelerations is now within reach.
Journal ArticleDOI
Affinity Chromatography And Metal Chelate Affinity Chromatography
TL;DR: A group of methods based on the molecular affinities found in biological systems have become increasingly important among separation procedures and are likely to be used for preparative isolation of proteins.
Journal ArticleDOI
Porcine carboxypeptidase B. Nitration of the functional tyrosyl residue with tetranitromethane.
TL;DR: In this paper, an active-site tyrosine residue was found to be a component of the active site region of bovine carboxypeptidase A with diazotized arsanilic acid.
References
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Journal ArticleDOI
Structure of hen egg-white lysozyme. A three-dimensional Fourier synthesis at 2 Angstrom resolution.
C. C. F. Blake,D. F. Koenig,D. F. Koenig,G. A. Mair,A. C. T. North,D. C. Phillips,V. R. Sarma +6 more
TL;DR: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 A Resolution as mentioned in this paper, 3D Fourier synthesis at 2 a resolution.
Journal ArticleDOI
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
J. C. Kendrew,R. E. Dickerson,B. E. Strandberg,R G Hart,D R Davies,D. C. Phillips,V. C. Shore +6 more
Journal ArticleDOI
Structure of papain.
TL;DR: A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft as mentioned in this paper.
Related Papers (5)
Metallocarboxypeptidases: stability constants and enzymatic characteristics.
Joseph E. Coleman,Bert L. Vallee +1 more