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- W2002072932 abstract "1. Arginase has been prepared from horse liver which exhibited one major component and a minor, slower-moving component upon electrophoresis at pH 7.35. Ultracentrifugal analysis also showed the presence of only two components, the lesser of which could be made to sediment as a pellet on the bottom of the cell. This material exhibited no enzyme activity. 2. From the ultracentrifugal analysis, provisional values were deduced for certain molecular constants of horse liver arginase, namely, s = 5.95 × 10−13 sec., molecular weight = 138,000, and ff0 = 1.47. 3. The amino acid composition of the purified arginase was determined by column chromatography. The results are those of a typical protein. 4. Study of the thermal stability of arginase in the presence of certain bivalent metal ions gave the following order for their stabilizing effect: Mn++ > Ni++ > Co++. 5. Arginase was found to be strongly inhibited by Zn++, but unaffected by Cd++." @default.
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- W2002072932 date "1956-06-01" @default.
- W2002072932 modified "2023-10-17" @default.
- W2002072932 title "Liver arginase. III. Properties of highly purified arginase" @default.
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- W2002072932 doi "https://doi.org/10.1016/0003-9861(56)90143-6" @default.
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