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- W1574681789 abstract "Dinitrophenylation of rabbit muscle and yeast glyceraldehydes-3-phosphate dehydrogenases modifies only SH groups. The rabbit muscle apoenzyme loses 75% of its original activity upon dinitrophenylation of two SH groups per tetramer whereas the yeast apoenzyme is totally inactivated under the same conditions. Dinitrophenylation of the active-site cysteine-149 of rabbit muscle and yeast holoenzymes results in an loss of activity corresponding to a ‘half-of-the-sites’ and a ‘full-sites’ reactivity respectively. Determination of the sulphydryl content of the modified enzyme shows an unmasking of the cysteine residues of the dinitrophenylated rabbit muscle apoenzyme which is not observed for the yeast protein. However, conformational changes are revealed for both dinitrophenylated apoenzymes by differential absorptin spectroscopy or by limited proteolysis. Sulphydryl group unmasking is not observed after modification is performed in the presence of two moles NAD +/ mole rabbit muscle enzyme. Although the apoenzyme is sensitive to an induced conformational change, our results favour symmetrical structures for both yeast ap and holo enzymes. The bis-dinitrophenylated rabbit muscle apoenzyme presents all the characteristics of an asymmetrical strycture; however, it is not possible to deduce whether this asymmetry is due to the chemical modification or whether it preexists in the native apoenzyme. The results of the dinitrophenylation of the rabbit holenzyme, however. Indicate that this enzyme possesses an asymmetrical structure." @default.
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- W1574681789 date "1981-10-01" @default.
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- W1574681789 title "Structure and Reactive Relationship in Glyeeraledehyde-3-Phosphate Dehydrogenase. Dinitrophenylation of Cysteine Residues of Yeast and Rabbit Muscle Enzymes" @default.
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- W1574681789 doi "https://doi.org/10.1111/j.1432-1033.1981.tb05653.x" @default.
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