Difficulties in the use of β-hydroxoaquotriethylene-tetraminecobalt(III) ion for sequential analysis of peptides
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference25 articles.
1. Hydrolytic Cleavage of N-Terminal Peptide Bonds by a Cobalt Chelate
2. Hydrolysis of N-Terminal Peptide Bonds and Amino Acid Derivatives by the β-Hydroxoaquotriethylenetetraminecobalt(III) Ion
3. Formation of peptide bonds in the coordination sphere of cobalt(III)
4. Cobalt(III)-promoted hydrolysis of chelated glycine amides, glycylglycine, and glycylglycine esters. Kinetics and mechanism
5. The kinetics of base hydrolysis of the peptide bond in the glycylglycine methyl ester complex of β-(triethylenetetramine)cobalt(III)
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. Hydrolysis and Condensation Reactions of O- and N-Bound Ligands;Reactions of Coordinated Ligands;1989
2. Cobalt(III)-promoted hydrolysis of amino acid esters and peptides and the synthesis of small peptides;Accounts of Chemical Research;1987-10-01
3. Structure and conformation analyses of two isomeric glycinato[tris-(2-aminoethyl)amine]cobalt(III) complex ions;Journal of the Chemical Society, Dalton Transactions;1976
4. Sequential hydrolysis of peptides with .beta.-hydroxoaquo triethylenetetraminecobalt(III) ion;Inorganic Chemistry;1974-04-01
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