Nucleoside Phosphotransferase from Carrot
نویسندگان
چکیده
منابع مشابه
Purification and properties of a nucleoside phosphotransferase from carrot.
A simple procedure affording a 940-fold purification of the nucleoside phosphotransferase from carrot is described. Preliminary evidence indicates that, by an additional fractionation through a Sephadex column, a further 5to 6-fold increase in activity can be effected. The particle weight of the enzyme varies with pH. At the pH optimum of 5.0 one species of particle weight 45,000, at pH 9.5 two...
متن کاملNucleoside phosphotransferase from carrot. Kinetic studies and exploration of active sites.
In the light of the kinetic studies reported in this paper, the nucleoside phosphotransferase of carrot is considered as an enzyme possessing two hydrolytic sites, binding the phosphate donor, and one transfer site, engaging the nucleoside acceptor. The purification of the protein used in these studies, with phenylphosphate as the donor and uridine as the acceptor, is described. In addition to ...
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Precoated cellulose thin-layer chromatograms were used to detect the production of guanosine 5'-phosphate from guanosine and p-nitrophenylphosphate by whole-cell preparations. One-hundred per cent of Serratia (163 strains) and 84% of E. liquefaciens (15 of 18 strains) produced the nucleotide. All other Enterobacter (23 strains), Klebsiella (10 strains), and E. coli (10 strains) were negative fo...
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The presence of multiple forms of enzyme with terminal action pattern on pectate was evaluated in the protein mixture obtained from carrot roots. The form with pH optimum 3.8 clearly preferred substrates with a lower degree of polymerization (oligogalacturonates). Its molecular mass, isoelectric point, glycosylation as well as cleavage of pectate from nonreducing end corresponded to an exopolyg...
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The evolutionary design of genetic switches and circuits requires iterative rounds of positive (ON-) and negative (OFF-) selection. We previously reported a rapid OFF selection system based on the kinase activity of herpes simplex virus thymidine kinase (hsvTK) on the artificial mutator nucleoside dP. By fusing hsvTK with the kanamycin resistance marker aminoglycoside-(3')-phosphotransferase (A...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62867-4