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- W2003990522 abstract "Isoenzymes of wheat germ acid phosphatase were separated into several fractions by DEAE-cellulose chromatography using a pH gradient. Disc electrophoresis indicated 7 separate isoenzymes. One DEAE-cellulose fraction, labeled as Group I, contained 4 of the 7 isoenzymes and another, labeled as Group II, contained the other 3. Sedimentation velocity analysis indicated that each group was monodisperse, as indicated by a single sedimenting peak. The 3rd and 7th isoenzymes (numbered on basis of electrophoretic migration) were isolated by further DEAE-cellulose chromatography. The absorption spectra of isoenzymes 3 and 7 were not alike but both indicate the presence of a metal. The isoenzymes 3 and 7 had similar pH optimum, but different substrate constants (Km) for o-carboxyphenylphosphate. Inhibition studies indicated that both isoenzymes 3 and 7 had about 2 · 103 times greater affinity for molybdate than for orthophosphate. Orthophosphate competitively inhibited the reaction of isoenzyme 3 with o-carboxyphenylphosphate." @default.
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- W2003990522 date "1973-04-01" @default.
- W2003990522 modified "2023-10-16" @default.
- W2003990522 title "Separation and characteristics of isoenzymes of wheat germ acid phosphatase" @default.
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- W2003990522 doi "https://doi.org/10.1016/0304-4211(73)90071-0" @default.
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