Serum esterases. II. An enzyme hydrolysing diethyl p-nitrophenyl phosphate (E600) and its identity with the A-esterase of mammalian sera.
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منابع مشابه
The differentiation of the A-type esterases in sheep serum.
The differentiation of paraoxonase (an A-type esterase in serum) from related enzymes has been complicated by overlapping substrate specificities and by the complex nature of these enzymes. Rabbit-serum paraoxonase has been differentiated from hog-kidney diisopropyl phosphorofluoridatase by Mounter (1954). He confirmed the observation of Aldridge (1953b) that one enzyme in rabbit serum hydrolys...
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activated the p-nitrophenyl acetateand p-nitrophenyl butyrate-hydrolysing activity of sheep serum at a significantly slower rate than it did the paraoxon-hydrolysing activity. From this and supporting evidence involving theKm for hydrolysis activity of sheep, rabbit and hog sera and of purified paraoxonase towards p-nitrophenyl acetate, it was concluded that a new esterase hydrolysing pnitrophe...
متن کاملTHE inhibition of chymotrypsin by diethyl p-nitrophenyl phosphate.
The alkyl fluorophosphonates were first shown in 1940 (Adrian, Feldberg & Kilby, 1947) to be very powerful inhibitors of cholinesterase, and for a time they were thought to be quite specific for this enzyme. Later, other esterases, such as human milk lipase and liver esterase (Webb, 1948) and citrus acetylesterase (Jansen, Nutting & Balls, 1947) were also shown to be inhibited, although not to ...
متن کاملAnalysis of tissue esterases from patients with Hodgkin's disease and other types of advanced cancer by isoelectric focusing in acrylamide gel.
the colon, adenocarcinoma of the breast) and on nonneoplastic tissues from cancer patients (liver, kidney, spleen, brain, and red blood cells). Eighteen distinct nonspecific esterase bands have been identified and characterized with respect to substrate preference and inhibitor profile. Each of the normal tissues contains a readily recognizable esterase pattern; the tumor extracts present great...
متن کاملModification of in vitro metabolism of T-2 toxin by esterase inhibitors.
In vitro metabolism of T-2 toxin with S-9 fraction obtained from livers of phenobarbital-treated pigs and rats in the presence of different esterase inhibitors, including NaF, p-hydroxymercuribenzoate, phenylmethylsulfonyl fluoride, eserine sulfate, diisopropylfluorophosphate, and diethyl p-nitrophenyl phosphate, was studied. The metabolism was completely shifted to the hydroxylation at the C-3...
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عنوان ژورنال:
- The Biochemical journal
دوره 53 1 شماره
صفحات -
تاریخ انتشار 1953