Metallocarboxypeptidases: stability constants and enzymatic characteristics.
Joseph E. Coleman,Bert L. Vallee +1 more
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This article is published in Journal of Biological Chemistry.The article was published on 1961-08-01 and is currently open access. It has received 197 citations till now.read more
Citations
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Book ChapterDOI
The Interpretation Of Hydrogen Ion Titration Curves Of Proteins
TL;DR: This chapter reviews that titration curves do not represent just another way of physically characterizing a protein molecule, and contains experimental procedures of general utility in the determination of titration data.
Journal ArticleDOI
Control of zinc transfer between thionein, metallothionein, and zinc proteins
TL;DR: It is shown that selenium compounds are potential cellular enhancers of zinc transfer from MT to apoenzymes and the cellular redox state as well as the concentration of other biological chelating agents might well determine the direction of zinctransfer and ultimately affect zinc distribution.
Book ChapterDOI
Free Radicals and Reactive Oxygen Species as Mediators of Heavy Metal Toxicity in Plants
TL;DR: In most plants, exposure to elevated concentrations of heavy metals results in growth inhibition (see Chap. 8). After prolonged metal exposure, sensitive plants develop visible symptoms of toxicity such as chlorosis and necrotic lesions.
Book ChapterDOI
Carboxypeptidase A: a protein and an enzyme.
TL;DR: This chapter discusses the relationship of the three-dimensional structures of bovine carboxypeptidase A, and of its complexes with substrates and inhibitors, to the functional behavior of this enzyme.
References
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Journal ArticleDOI
Hydrogen Ion Equilibria of Bovine Serum Albumin1
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The Nature of the Amino Acid Residues Involved in the Inactivation of Ribonuclease by Iodoacetate
TL;DR: The fact, that the pH optimum for the reaction leading to the formation of imidazole carboxymethyl ribonuclease is around pH 5.5 to 6, instead of at the more alkaline pH values observed for the alkylation of cy-N-acetylhistidine, suggests that inactivation takes place as a result of substitution on a particular one of the four histidine residues present in rib onuclease.
Journal ArticleDOI
Quantitative studies of the avidity of naturally occurring substances for trace metals. 2. Amino-acids having three ionizing groups
Journal ArticleDOI
Hydrogen Ion Equilibria of Ribonuclease1
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