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- W2072004170 abstract "After treatment of ATP creatine transphosphoryla.se with maleic or succinic anhydride, the enzyme was purified using Sephadex G‐25 and the number of s‐lysine groups that reacted determined by utilization of radioactive maleic anhydride, U. V. spectroscopy, titration of succinic acid liberated upon hydrolysis, and by dinitrophenylation. Before exposure to hydroxylamine, about J 20 moles anhydride were bound per mole of protein ; and after exposure, about 68 moles remained ligated. Low speed sedimentation equilibrium experiments showed that maleylation induced formation of subunits of molecular weight half that of the original molecule. After digestion of the maleylated protein with trypsin, the resulting peptides were separated on a Dowex column, followed by high voltage electrophoresis and paper chromatography. Twenty‐two spots were obtained, all of which were positive when sprayed with Sakaguchi reagent." @default.
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- W2072004170 date "1970-12-01" @default.
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- W2072004170 title "STUDIES ON SUCCTNYLATED and MALEYLATED ATP: CREATINE PHOSPHOTRANSFERASE" @default.
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- W2072004170 doi "https://doi.org/10.1111/j.1399-3011.1970.tb01680.x" @default.
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