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- W2362114493 abstract "The stabilities of snake and rabbit muscle glyceraldehyde-3-phosphate dehydrog-enases(GAPDH)were compared.It was found that the snake enzyme is more stableto heat than the rabbis enzyme.The melting point of snake muscle apo-GAPDH is62.5℃,but the melting point of rabbit muscle apo-GAPDH is 52.5℃.At 55℃ therate of heat inactivation of snake musole apo-GAPDH is much smaller than that ofrabbit muscle apo-GAPDH.Snake muscle apo-GAPDH loses half of its activity in1.2 hour,but the half times for rabbit muscle apo-GAPDH and holo-GAPDH arerespectively 1.4 and 2.6 minutes.Heat inactivation for both enzymes is a first orderreaction.The rate of heat inactivation decreases in the presence of substrates.Theprotective effect of NAD~+ is the strongest.When the ratio of NAD~+ to enzyme is 240,She rates of heat in activation of snake and rabbit muscle GAPDH were reduced 32and 165 fold,respectively,but the snake enzyme is still more stable than the rabbitenzyme.The optimum pH of snake and rabbit muscle GAPDH is the same,but thesnake muscle enzyme is more stable towards changes in pH.The range of stabilityfor the snake muscle apo-enzyme is pH 4.9~9.4,but for the rabbit muscle apo-enzyme,it is pH 6.1~8.1. At 0℃ ATP induces also inactivation of snake muscleGAPDH,but the rate of inactivation for the snake muscle enzyme is lower than thatfor the rabbit muscle enzyme.The results indicate that snake muscle GAPDH ismore stable than rabbit musole GAPDH,the structure of snake muscle GAPDH ismore rigid than rabbit muscle GAPDH,the affinity between subunits of snakemuscle GAPDH is stronger than rabbit musole GAPDH." @default.
- W2362114493 created "2016-06-24" @default.
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- W2362114493 date "1982-01-01" @default.
- W2362114493 modified "2023-09-25" @default.
- W2362114493 title "STUDIES ON SNAKE MUSCLE GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE——II.COMPARISON OF STABILITIES BETWEEN SNAKE AND RABBIT MUSCLE GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES" @default.
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