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- W1965585461 abstract "The purification of carbamyl phosphate-l-ornithine transcarbamylase (carbamyltransferase) from pea seedlings is described. The enzyme was purified approximately 2000-fold with a yield of 32%. Column electrophoresis yielded a fraction which represented a 4000-fold purification. The optimal pH was found to be 8.45. The enzyme was found to be highly specific for l-ornithine with only slight activity with d-ornithine. Sodium fluoride, p-hydroxymercuribenzoate, and chloroacetophenone inhibited the enzyme. EDTA restored about 85% of the activity inhibited by p-hydroxymercuribenzoate. High concentrations of l-ornithine were effective in overcoming the inhibitory effect of chloroacetophenone. The sedimentation constant, s20,w, for the purified enzyme (before column electrophoresis) was found to be 5.48." @default.
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- W1965585461 date "1964-08-01" @default.
- W1965585461 modified "2023-10-18" @default.
- W1965585461 title "Purification of ornithine transcarbamylase from pea seedlings" @default.
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- W1965585461 doi "https://doi.org/10.1016/0003-9861(64)90329-7" @default.
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