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- W2073397105 abstract "Abstract 1. 1. AMP-aminohydrolase has been purified from skeletal muscle of chick embryo, I-day-old chick, and adult hen. 2. 2. The reaction rates measured at low substrate concentrations (5.5 × 10 −5 M ) at temperatures between 10 and 50° C. showed that ‘ adult ’ enzyme has a temperature optimum of 35° C., whereas ‘ embryonic ’ enzyme has no temperature optimum in this temperature range, the rate increasing steadily with the rise of temperature. 3. 3. The dependence of K m on temperature was different for ‘ adult’ and for ‘ embryonic ’ enzyme, indicating that the differences mentioned above consist of different enzymesubstrate affinity rather than of different molecular activity of the enzyme." @default.
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- W2073397105 date "1971-02-01" @default.
- W2073397105 modified "2023-09-27" @default.
- W2073397105 title "Differencs in therma susceptibility of the kinetics of amp-aminohydrolase from foetal and postnatal chick muscl" @default.
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- W2073397105 doi "https://doi.org/10.1016/0020-711x(71)90037-1" @default.
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