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- W2059125532 abstract "Branched-chain amino acid aminotransferase (BCAT) was partially purified from 4-day-old barley seedlings. The enzyme activity was assayed using radioactive amino acids. Enzyme activity changes during germination of barley were investigated. The most suitable keno acid for the enzyme was 2-oxoglutarate. Addition of leucine, valine, isoleucine or glutamate to the enzyme extract decreased the heat stability of the enzyme. The molecular weight of barley BCAT was about 95,000 daltons and optimum pH was about 8.4. Km values for the substrates are such that the enzyme can operate in both directions. The role of BCAT in biosynthesis and catabolism of branched-chain amino acids is discussed." @default.
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- W2059125532 date "1981-05-01" @default.
- W2059125532 modified "2023-10-16" @default.
- W2059125532 title "Branched-chain Amino Acid Aminotransf erase in Barley Seedlings" @default.
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- W2059125532 doi "https://doi.org/10.1016/s0044-328x(81)80219-x" @default.
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