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- W1498581838 abstract "The two primary forms of transaldolase present in commercial strains of Candida utilis are identical in enzymatic properties but differ in amino acid composition, molecular weight, and stability to heat inactivation. Each isoenzyme appears to contain two identical polypeptide chains, and a mixture of the two primary forms yields a hybrid form containing both polypeptide chains. The equilibrium constant for formation of the hybrid form from the parental forms is 0.66. Hybridization studies have also been carried out with the corresponding β-glyceryl derivatives formed by reduction of the intermediate Schiff-base complexes. Hybrids are not formed if both isoenzymes are in the β-glyceryl form, but if only one isoenzyme has been converted, then hybridization follows the predicted pattern, yielding the hybrid isoenzyme with 50% of the original activity. There is an equal contribution from each parental protein in the formation of the hybrid." @default.
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- W1498581838 date "1970-01-01" @default.
- W1498581838 modified "2023-09-26" @default.
- W1498581838 title "Isoenzymes of transaldolase in Candida utilis" @default.
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- W1498581838 doi "https://doi.org/10.1016/0003-9861(70)90354-1" @default.
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