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- W1629582552 abstract "The kinetics and mechanism of action of a partially purified hexokinase from rat skeletal muscle tissue were investigated. The enzyme was isolated after a series of ammonium sulfate fractionations and chromatography on diethylaminoethyl cellulose. Initial rate experiments revealed a fundamental difference between this enzyme, which is referred to as muscle hexokinase II, and another hexokinase present in muscle tissue. These observations are consistent with the demonstration by Katzen and Schimke of the existence of two hexokinase isozymes in rat skeletal muscle tissue (3). The mechanism of action of muscle hexokinase II appears to be of the rapid equilibrium random type, i.e. random addition of substrates to the enzyme, where all enzyme and substrate interactions equilibrate rapidly relative to interconversion of the central ternary complexes, enzyme-adenosine triphosphate-glucose and enzyme-adenosine diphosphateglucose 6-phosphate. The other hexokinase present in muscle tissue exhibits a reaction mechanism in which a substrate reacts with the enzyme to produce a product prior to the addition of the second substrate. Kinetic experiments with AMP, ADP, mannose, and mannose-6-P suggest that muscle hexokinase II is similar, but not identical, in its mechanism of action to yeast hexokinase, pyruvate kinase, and creatine kinase." @default.
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- W1629582552 date "1967-02-01" @default.
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- W1629582552 title "Rat Skeletal Muscle Hexokinase" @default.
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- W1629582552 doi "https://doi.org/10.1016/s0021-9258(18)96301-5" @default.
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