Concurrent Bromoacetate Reaction at Histidine and Methionine Residues in Ribonuclease
نویسندگان
چکیده
منابع مشابه
Alkylation and identification of the histidine residues at the active site of ribonuclease.
The reactions of iodoacetate and bromoacetate with ribonuclease have already provided some information on the relationship between the chemical structure and the catalytic a(*tivity of the enzyme. It is the purpose of this and the following paper to extend this information. In earlier studies, Gundlach, Stein, and Moore (1) showed that although alkylation at lysine, mrthioninc, or histidine res...
متن کاملProperties and conformation of the histidine residues at the active site of ribonuclease.
The formation, isolation, and characterizat,ion of two isomeric, inactive derivatives of ribonuclease, l-carboxymethylhistidinc119and 3-carboxymethylhistidine-12-ribonuclease,1 were dcscribed in the preceding paper (2). Studies on the course of the alkylation reaction and on some of the properties of the two alkylated derivatives are the subject of the present communication. It has been found t...
متن کاملFurther studies on the alkylation of the histidine residues at the active site of pancreatic ribonuclease.
The chemistry of the active site of bovine pancreatic ribonuclease has been further examined by study of the reaction of iodoacetic acid with histidine residues 12 and 119 in derivatives of the protein. In the native enzyme, the stereospecific alkylation of the two imidazole rings is a mutually exclusive, electrostatically oriented reaction leading to a 7 : 1 ratio of substitution at residues 1...
متن کاملReaction of ethylene oxide with histidine, methionine, and cysteine.
Since it was shown (2) that the treatment of casein with ethylene oxide could diminish the biological availability of the histidine and methionine of this protein, it became of interest to determine whether other proteins were affected in the same way and to elucidate the nature of the chemical reactions involved. Particular interest in such reactions derives from the use of ethylene oxide as a...
متن کاملContribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58----Ala.
The pK values of the histidine residues in ribonuclease T1 (RNase T1) are unusually high: 7.8 (His-92), 7.9 (His-40), and 7.3 (His-27) [Inagaki et al. (1981) J. Biochem. 89, 1185-1195]. In the RNase T1 mutant Glu-58----Ala, the first two pK values are reduced to 7.4 (His-92) and 7.1 (His-40). These lower pKs were expected since His-92 (5.5 A) and His-40 (3.7 A) are in close proximity to Glu-58 ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1967
ISSN: 0006-2936
DOI: 10.1042/bj1020007c