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- W2000503518 abstract "Numerous detailed reports regarding aspartate aminotransferase (EC 2.6.1.1) from animal tissues have demonstrated a requirement for pyridoxal-5-phosphate which acts as a coenzyme. Evidence for this has been largely based on studies with the purified and resolved enzyme (e.g. O'Kane and Gunsalus, 1947; Cammarata and Cohen, 1951; Meister et al., 1954). Although aspartate aminotransferase is known to occur in higher plants (Smith and Williams, 1951; Cook, 1957; Cruickshank and Isherwood, 1958; Patwardhan, 1960; Ellis and Davies, 1961; Fasella et al., 1966), complete resolution of the holoenzyme has not been reported. However considerable indirect evidence suggests that the plant enzyme is pyridoxal phosphate dependent (Cruickshank and Isherwood, 1958; Davies and Ellis, 1961). In this communication the resolution of aspartate aminotransferase from germinating pea cotyledons and its absolute requirement for pyridoxal and pyridoxamine phosphates is demonstrated." @default.
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- W2000503518 date "1966-12-01" @default.
- W2000503518 modified "2023-09-27" @default.
- W2000503518 title "Resolution of aspartate aminotransferase from a higher plant source" @default.
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- W2000503518 doi "https://doi.org/10.1016/0006-291x(66)90504-3" @default.
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