Abstract:
:Rat serum carboxylesterase [carboxylic ester hydrolase, EC 3.1.1.1] was purified by ammonium sulfate precipitation, chromatography on DEAE-cellulose, QAE Sephadex A-50 and brushite, and gel filtration on Sephadex G-200. This purified enzyme was shown to be a single protein band on slab gel electrophoresis and its final specific activity was 49.5 units/mg protein. This enzyme was very sensitive to diisopropylfluorophosphate (DFP) but not to p-chloromercuribenzoate (PCMB), eserine, o-iodosobenzoate, NaF or ethylenediamine tetraacetic acid (EDTA). The pH profile of the reactions catalysed by this enzyme showed broad optimum between pH 6.0 and 8.8. The activity of purified enzyme was not affected by Ca2+, Mg2+, Mn2+, Cu2+, Zn2+, Co2+, and Cd2+ at 1 mM concentration. The molecular weight measured by gel filtration was approximately 84,000 and the isoelectric point was 4.4. The enzymatic properties were not changed by neuraminidase treatment with regard to heat stability, pH optimum, sensitivity to metal ions and inhibitors, and Km values for p-nitrophenylesters of different acyl C-chain length.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Hashinotsume M,Higashino K,Hada T,Yamamura Ydoi
10.1093/oxfordjournals.jbchem.a132254subject
Has Abstractpub_date
1978-12-01 00:00:00pages
1325-33issue
6eissn
0021-924Xissn
1756-2651journal_volume
84pub_type
杂志文章abstract::Proteoglycan biosynthesis in developing chicken corneas was studied. Corneas free of scleral rims were prepared from 5- to 18-day-old chick embryos and labeled in vitro with [3H]glucosamine and [35S]sulfate. Then, the labeled medium and corneal proteoglycans were analyzed. Day 5 corneas synthesized mainly chondroitin ...
journal_title:Journal of biochemistry
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pub_type: 杂志文章
doi:10.1093/jb/mvg171
更新日期:2003-10-01 00:00:00
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更新日期:1993-06-01 00:00:00
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