Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Reinhard G. Kleineidam"'
Publikováno v:
Glycoconjugate Journal. 14:57-66
The inhibition of the α-2,6-sialyltransferase from rat liver, the α-2,3-sialyltransferase from porcine submandibular gland and of the galactosyltransferase from human milk were studied using monosaccharide-, nucleoside- and nucleotide-derivatives o
Autor:
Johannes F.G. Vliegenthart, Hans-Christian Siebert, Susanne Kruse, Jaap J. Beintema, Christine S. Wright, Robert Kaptein, Johannis P. Kamerling, Roland Schauer, Ukun M.S. Soedjanaatmadja, Hans-Joachim Gabius, Reinhard G. Kleineidam, Ann C. Rice, Petra J. W. Pouwels
Publikováno v:
Glycoconjugate Journal. 14:531-534
The side chains of tyrosine, tryptophan and histidine are able to produce CIDNP (Chemically Induced Dynamic Nuclear Polarization) signals after laser irradiation in the presence of a suitable radical pair-generating dye. Elicitation of such a respons
Publikováno v:
Biological Chemistry Hoppe-Seyler. 376:569-576
Clostridium perfringens produces two sialidases, one of which has a molecular mass of 71 kDa and is secreted, while the 'small', 43 kDa isoenzyme remains in the cells. The secreted, higher molecular mass sialidases of two different clostridial strain
Publikováno v:
Glycoconjugate Journal. 10:116-119
Fractionation of horse liver homogenate by centrifugation into heavy membranes at 10,000 x g, microsomal fraction at 105,000 x g, and the supernatant revealed sialate 9-O-lactoyltransferase activity only in the latter fraction. For the enzyme assay,
Publikováno v:
ChemInform. 22
Publikováno v:
Glycoconjugate Journal. 9:235-240
Three site-specific mutations were performed in two regions of a sialidase gene from Clostridium perfringens which are known to be conserved in bacterial sialidases. The mutant enzymes were expressed in Escherichia coli and, when measured with MU-Neu
Autor:
Reinhard G. Kleineidam, Michael Hartmann, Erwin Schreiner, R. Christian, Roland Schauer, Erich Zbiral
Publikováno v:
Biochemical Journal. 282:511-516
A series of neuraminic acid derivatives modified in the side chain or at C-3, C-4 or C-5 were tested as substrates of inhibitors of N-acetylneuraminate lyase (EC 4.1.3.3) from Clostridium perfringens. The results, together with Km and Ki values repor
Publikováno v:
Trends in Glycoscience and Glycotechnology. 4:263-268
シアリダーゼ (ノイラミニダーゼEC3.2.1.18)は、ガス壊疽菌である Clostridium により多量に産生され、哺乳動物組織の崩壊の一翼を担うことにより、その病原性に重要な役割を演ずる。シア
Publikováno v:
Liebigs Annalen der Chemie. 1991:129-134
The peracetylated methyl ester 1 of N-acetylneuraminic acid was transformed into the oxazoline derivative 2, which was hydrogenated with Pd/C/H2 to give the 4-deoxy-Neu5Ac2en derivative 3. Acid cleavage of the oxazoline 2 by trifluoroacetic acid (THF
Publikováno v:
Biological Chemistry Hoppe-Seyler. 371:715-720
4-O-Acetylated, 7-O-acetylated, and 9-O-acetylated 4-methylumbelliferyl-alpha-N-acetyl-neuraminic acids (Neu4,5Ac2-MU, Neu5,7Ac2-MU, Neu5,9Ac2-MU) were tested as substrates of sialidases of Vibrio cholerae and of Clostridium perfringens. Both sialida