Zobrazeno 1 - 7
of 7
pro vyhledávání: '"J E, Dotzlaf"'
Publikováno v:
Journal of Biological Chemistry. 266:5087-5093
Deacetoxycephalosporin C hydroxylase from cell-free extracts of Streptomyces clavuligerus was stabilized partially and purified to near homogeneity by three anion-exchange chromatographies, ammonium sulfate fractionation, and two gel filtrations. The
Publikováno v:
The Journal of biological chemistry. 269(16)
Intrinsic resistance toward beta-lactams in methicillin-resistant Staphylococcus aureus strains, a major source of nosocomial infections, is believed to be caused mainly by penicillin-binding protein 2a (PBP2a). This protein resembles other penicilli
Publikováno v:
The Journal of biological chemistry. 266(8)
Deacetoxycephalosporin C hydroxylase from cell-free extracts of Streptomyces clavuligerus was stabilized partially and purified to near homogeneity by three anion-exchange chromatographies, ammonium sulfate fractionation, and two gel filtrations. The
Publikováno v:
Bulletin of Environmental Contamination and Toxicology. 13:357-361
Tha degradation of chlorinated benzoates by natural microbial populations has been reported to occur in the ~bsence of additional carbon and/or energy sources by a co-metabolic process (HORVATH 1973; HO~VATH 1972a; HORVATH 1972b; HORVATH 1971). Howev
Publikováno v:
The Journal of biological chemistry. 263(30)
S-Adenosyl-L-methionine:macrocin O-methyltransferase catalyzes conversion of macrocin to tylosin, the terminal and main rate-limiting step of tylosin biosynthesis in Streptomyces fradiae. The O-methyltransferase was stabilized in vitro and purified t
Autor:
Wu-Kuang Yeh, J. E. Dotzlaf
Publikováno v:
Journal of bacteriology. 169(4)
Deacetoxycephalosporin C synthetase (expandase), which catalyzes ring expansion of penicillin N to deacetoxycephalosporin C (DAOC), has been stabilized in vitro and purified to near homogeneity from the industrially important fungus Cephalosporium ac
Autor:
J E, Dotzlaf, W K, Yeh
Publikováno v:
The Journal of biological chemistry. 264(17)
A putatively rate-limiting synthase (expandase) of Streptomyces clavuligerus was stabilized in vitro and purified 46-fold from cell-free extracts; a major enriched protein with a Mr of 35,000 was further purified by electrophoretic elution. Based on