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- W1244179074 abstract "This chapter illustrates the assay, purification, and properties of carbamate kinase. The activity of the enzyme in the synthesis of carbamyl phosphate is measured by quantitatively converting the carbamyl phosphate to citrulline in the presence of ornithine and ornithine transcarbamylase. One unit of carbamate kinase refers to the amount that catalyzes the synthesis of 1 micromole of carbamyl phosphate per minute at 37°. The buffers for the purification procedure are made up in deionized water. Either “enzyme grade” ammonium sulfate or ammonium sulfate recrystallized from a slightly alkaline solution of EDTA is used. On electrophoresis in starch gel at pH 7.0, the enzyme migrates toward the anode with only a trace of an impurity detectable in the crystalline preparation. The requirement of carbamate kinase for a divalent cation can be met by Mg2+, Mn2+, and Co2+. The crystalline enzyme catalyzes reactions with both acetate and acetyl phosphate at about 0.03, the rate with carbamate and carbamyl phosphate, respectively. It also acts as an ATPase in the presence of bicarbonate and Mn2+ at a rate 0.003 that with carbamate." @default.
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- W1244179074 date "1970-01-01" @default.
- W1244179074 modified "2023-09-23" @default.
- W1244179074 title "[21] Carbamate kinase (Streptococcus faecalis)" @default.
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- W1244179074 doi "https://doi.org/10.1016/0076-6879(71)17186-8" @default.
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