Carbohydrate Metabolism - Part E by Willis A. Wood (Eds.)
By Willis A. Wood (Eds.)
The severely acclaimed laboratory regular, Methods in Enzymology, is likely one of the such a lot hugely revered guides within the box of biochemistry. considering the fact that 1955, each one quantity has been eagerly awaited, often consulted, and praised through researchers and reviewers alike. The sequence comprises a lot fabric nonetheless correct this present day - really an important book for researchers in all fields of lifestyles sciences
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Extra resources for Carbohydrate Metabolism - Part E
A divalent metal ion is required for the glucokinase reaction. The following rates of D-glucose phosphorylation were observed in the presence of 10 mM metal salts: Co 2÷, 264; Mn 2÷, 173; Mg z+, 100; Cd 2+, 91; Zn z+, 56; Fe z+, 47; Ca 2+, 34; Sr 2+, 11; and Cu 2+, < 1. Inhibition Studies. 71 mM), respectively. 31 raM) at saturating ATP. 01 mM) of glucose utilization, respectively. 89 mM) of glucose utilization. pH Optimum. 5) buffers with overlapping at the transition pH values. 5. Stability. When stored at - 2 0 ° in the presence of 1 mM DTT and 20-30% glycerol, glucokinase preparations are stable indefinitely.
The molecular weight determined by SDS-polyacrylamide gel electrophoresis was also 58,000, showing that the enzyme contains a single polypeptide chain. The results of zone sedimentation on a sucrose gradient and molecular sieve chromatography confirmed the 58,000 Mr for the catalytically active galactokinase. The amino acid composition is given in Table II, and the N-terminal sequence is NHz-Thr-Lys-Ser-His-Arg-Glu-Arg-Val-Ile-Val-Pro. . I Glu Catalysis'. 0. The enzyme D. H. Schlesinger, M. A.
94 M. 39 M is reached. 76 M ammonium sulfate to precipitate the protein. 3 zate is centrifuged at 16,000 g for 20 min, and the supernatant solution is discarded. S e p h a d e x G-200 Chromatography. 1 M glucose. 5 cm × 90 cm Sephadex G-200 column that has been equilibrated in the a b o v e buffer. Two-milliliter fractions are collected, and those containing maxim u m hexokinase activity are pooled. The e n z y m e is precipitated by dialysis for 2 hr against saturated a m m o n i u m sulfate. The precipitated protein is centrifuged at 16,000g for 20 min and redissolved in 1 ml of the buffer.