The effect of limited proteolysis on rabbit muscle creatine kinase
نویسندگان
چکیده
منابع مشابه
Crystal structure of rabbit muscle creatine kinase.
The crystal structure of rabbit muscle creatine kinase, solved at 2.35 A resolution by X-ray diffraction methods, clearly identified the active site with bound sulfates surrounded by a constellation of arginine residues. The putative binding site of creatine, which is occupied by a sulfate group in this analysis, has been tentatively identified. The dimeric interface of the enzyme is held toget...
متن کاملThe reaction of rabbit muscle creatine kinase with diethyl pyrocarbonate.
The reaction of rabbit muscle creatine kinase with diethyl pyrocarbonate was studied. It was found that up to five of the sixteen histidine groups per enzyme subunit could be modified, and under the conditions employed, there was no evidence for formation of the disubstituted derivative of histidine. Evidence was obtained for small but significant amounts of modification of lysine and cysteine ...
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carbonic anhydrase III with an estimated purity of greater than 95%, as judged by electrophoresis in sodium dodecyl sulphate/polyacrylamide gels. Ion-exchange chromatography and salt fractionation were used to purify the bovine carbonic anhydrase 111. Bovine muscle was homogenized and adjusted t o 40% saturation with (NH4)*S04. The supernatant was applied t o a DEAE-cellulose column (2.5cm x 25...
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15 صفحه اولProbing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis
Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1981
ISSN: 0264-6021
DOI: 10.1042/bj1990239