نتایج جستجو برای: acetylgalactosamine
تعداد نتایج: 1087 فیلتر نتایج به سال:
UDP-galactose 4'-epimerase (GALE) interconverts UDP-galactose and UDP-glucose in the final step of the Leloir pathway. Unlike the Escherichia coli enzyme, human GALE (hGALE) also efficiently interconverts a larger pair of substrates: UDP-N-acetylgalactosamine and UDP-N-acetylglucosamine. The basis of this differential substrate specificity has remained obscure. Recently, however, x-ray crystall...
A UDP-N-acetylgalactosamine:globoside a-3-N-acetylgalactosaminyltransferase has been purified over 3500-fold in 4% yield from a Triton X-100 extract of canine spleen microsomes by affinity chromatography on globoside acid-agarose. Sodium dodecyl sulfate gel electrophoresis of the purified enzyme revealed two major bands with molecular weights of 66,000 and 56,000. Judging from the molecular wei...
In the title compound, [Ho(C(6)H(12)Cl(3)N(3)O(2)P)(3)(C(18)H(15)OP)], the Ho(III) ion is surrounded by six O atoms from the three bidentate N-[bis-(dimethyl-amino)phosphino-yl]-2,2,2-trichloro-acetamido ligands (L(-)) and by one O atom from the triphenyl-phosphine oxide ligand, with the formation of a distorted monocapped octa-hedron. In one ligand L(-), the trichloro-methyl group is rotationa...
Sir: Nagstatin (1) is a novel A^-acetyl-jft-D-glucosaminidase inhibitor isolated from culture nitrates of Streptomyces amakusaensis, and is structurally a nitrogenous 7V-acetylgalactosamine analog fused with an imidazole ring.1} Recently, we have synthesized de-branched nagstatin analogs having different configurations and functionalities, and then determined the absolute structure of nagstatin...
Gene expression analysis by microarray assay revealed that when exposed to stress, Entamoeba histolytica exhibits a specific heat shock response, together with a dramatic overall reduction in gene transcription as well as differential allelic expression of key genes participating in virulence, such as the galactose/N-acetylgalactosamine (Gal/GalNAc) lectin.
The detailed structures of the three asparagine-linked carbohydrate units of ovine lutropin subunits alpha and beta (oLH-alpha and oLH-beta) have been determined by carrying out the structural analysis on the three glycopeptides alpha GP-1, alpha GP-2, and beta GP-3, and the oligosaccharide obtained by alkaline sodium borohydride treatment of oLH and the individual subunits. Based on the result...
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