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- W2138870174 abstract "Several pituitary preparations from various species, including two purified follicle-stimulating hormone preparations, inhibited the D-glyceraldehyde-3-phosphate dehydrogenase reaction. The active factor in those preparations that caused the apparent inhibition has been identified as an enzyme, triose phosphate isomerase. Using D-glyceraldehyde-3-phosphate as the substrate, the optimum pH for the isomerization reaction is 8.4. The partially purified enzyme has a specific activity of 34 μmol dihydroxyacetone phosphate isomerized × min−1× mg protein−1. The Km of the enzyme for D-glyceraldehyde 3-phosphate is 0.79 mM, and the Km for dihydroxyacetone phosphate is 1.53 mM. Half of the enzyme activity is lost in 7 min at 55°C. The molecular weight of the enzyme is estimated to be 56000. The electrophoretic mobility of the enzyme differs from that of the muscle enzyme supplied by Sigma indicating a difference in amino acid composition between the two enzymes. Electrophoresis revealed the presence of two to three isozymes of the pituitary triose phosphate isomerase." @default.
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- W2138870174 date "1972-01-01" @default.
- W2138870174 modified "2023-10-16" @default.
- W2138870174 title "Identification and Characterization of Pituitary Triose-Phosphate Isomerase" @default.
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- W2138870174 doi "https://doi.org/10.1111/j.1432-1033.1972.tb19701.x" @default.
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