Photolabeling reagent for thiol enzymes. Studies on rabbit muscle creatine kinase.

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Effects of temperature and reagent size on the reaction of the thiol groups of rabbit muscle creatine kinase [proceedings].

The dimeric enzyme creatine kinase (EC 2.7.3.2) from rabbit muscle has a reactive thiol group on each subunit, modification of which by iodoacetate or iodoacetamide leads to inactivation of the enzyme (Watts, 1973). It had been previously shown (Price & Hunter, 1976) that when the enzyme is treated with iodoacetate or some other reagents in the presence of the 'transition-state analogue' comple...

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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...

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NOVEL REAGENTS FOR CREATINE KINASE

The purpose of this investigation was to develop a simple colorimetric method for creatine kinase (CK). The new method is based on the reaction of creatine, formed enzymatically from creatine phosphate and ADP, with different glyoxal compounds. Hydrated glyoxals, such as para-nitrophenyl, 2-thiophene, 4- biphenyl, 4, 4' -biphenyl,α-naphthyl, β-naphthyl, para-chlorophenyl, and styryl were...

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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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The 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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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1977

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(17)40263-8