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- W2024076395 abstract "Studies on the oxidative fraction obtained by chymotrypsin hydrolysis of glyceraldehyde-3-phosphate dehydrogenase A limited proteolysis of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase (d-glyceraldehyde-3-phosphate: NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12) by α-chymotrypsin (EC 3.4.4.5) causes a preferential loss of its phosphorylating and arsenolytic activities but oxidative activity is maintained. Besides dehydrogenase properties, the native enzyme possesses various other catalytic functions such as esterolytic, phosphatase activities and NADH-X formation. We have observed that, during the disappearance as the phosphorolytic and arsenolytic activities, the esterolytic, phosphatase, and NADH-X properties are much more stable and are maintained at the same level of oxidative activity. By passing the digested enzyme through a chromatographic column of Sephadex G-100 two active peaks, A and B, were separated. Peak A had the same chromatographic and enzymic properties as the native enzyme; in Peak B, where arsenolytic and phosphorolytic activities had disappeared, the oxidative and esterolytic activities were still present; the molecular weight of this fraction based on elution volume was estimated as 60 000 to 70 000. The fluorescence spectrum of Fraction B was displaced towards the visible by 15 mμ as compared with the native enzyme. The activity of Peak B was more stable in the presence of high concentration of NAD+ than without. The esterolytic activity was no longer inhibited by NAD+; and NADH does not have a limiting effect on the rate of oxidation. These data confirm previous kinetic results with native enzyme in which the oxidative and esterolytic activities were located on the same site; from the enzymic" @default.
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- W2024076395 date "1968-11-01" @default.
- W2024076395 modified "2023-09-27" @default.
- W2024076395 title "Étude de la fraction oxydante de la glycéraldéhyde-3-phosphate déshydrogénase obtenue par hydrolyse chymotrypsique" @default.
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- W2024076395 doi "https://doi.org/10.1016/0005-2744(68)90041-7" @default.
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