Detail of "35890-39-2"

Reference

Galectin-1 from bovine spleen: biochemical characterization, carbohydrate specificity and tissue-specific isoform profiles

Galectin-1 from bovine spleen: biochemical characterization, carbohydrate specificity and tissue-specific isoform profiles. Ahmed, Hafiz; Fink, Nilda E.; Pohl, Jan; Vasta, Gerardo R. (Cent. Marine Biotechnology, Univ. Maryland Biotechnology Inst.Several substances are used for example 5077-31-6 and 35890-39-2 which are their cas registry numbers., Baltimore, MD 21202, USA). Journal of Biochemistry (Tokyo), 120(5), 1007-1019 (English) 1996 Japanese Biochemical Society. CODEN: JOBIAO. ISSN: 0021-924X. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Selected biochem. properties, including the charge heterodispersity profile and carbohydrate specificity, of bovine galectin-1 were detd. in detail. The lectin was purified through an improved purifn. protocol that yielded 35-40 mg/kg of wet tissue with a specific activity of 1.7.2′104 mg-1.ml. The galectin is a homodimer of approx. 14.5 kDa subunits with E280mg/ml of 0.65 mL.mg-1.cm-1. When stored in the presence of its carbohydrate ligand, the lectin's binding activity remained stable in a non-reducing environment even at room temp. The optimal pH for binding to the ligand was 6.5-8.0. The overall carbohydrate specificity of the bovine galectin-1 isolated from spleen is similar to that of the galectin isolated from heart and to other mammalian galectins that exhibit "conserved" (Type I) carbohydrate recognition domains (CRDs) [Ahmed, H. and Vasta, G. R. (1994) Glycobiol. 4, 545-549], but differs from those from Xenopus laevis and rat intestine domain I. The fluorescence of 4-methylumbelliferyl a-D-galactopyranoside was quenched on binding to bovine spleen galectin-1. Scatchard plots of data obtained at 5, 15, and 30° showed that the galectin has two sugar exothermic binding sites with assocation consts. of 3.4′105, 1.0′105, and 0.3′105, resp. Chem. modification studies indicated that histidine, tryptophan, carboxylic acid, and arginine, but not lysine or tyrosine, are involved in the binding to the carbohydrate ligand. On isoelec. focusing, the spleen galectin-1 appeared as six isoforms ranging from pI 4.56-4.88 with main components at pI 4.63 (34.0%), 4.73(42.6%), and 4.88 (16.6%). The galectin-1 isolated from heart yielded a quali- and quant. different profile with four isoforms ranging from pI 4.53-4.73, those with pIs of 4.56, 4.63, and 4,73 being common to the spleen homolog. Edman degrdn. of selected peptides purified from the spleen galectin-1 digest revealed amino acid sequences identical to those obtained for the heart galectin-1. This suggest that although point mutations in the subunit primary structure may not be the likely source of isolectins, as obsd. for X. laevis tissue-specific co- or post-translational modifications may be the possible cause of the differences in the galectin isoform profile between bovine spleen and heart. .

Specificity of neuraminidase activity from Influenza viruses isolated in different hosts tested with novel substrates

Specificity of neuraminidase activity from Influenza viruses isolated in different hosts tested with novel substrates. Katinger, D.; Mochalova, L.; Chinarev, A.; Bovin, N.; Romanova, J. ( Polymun Scientific GmbH, Vienna, Austria). Archives of Virology, 149(11), 2131-2140 (English) 2004 Springer Wien. CODEN: ARVIDF. ISSN: 0304-8608. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Section cross-reference(s): 10 Influenza A and B viruses isolated in Vero and Madin Darby canine kidney (MDCK) cells as well as in fertilized hen eggs were tested for the specificity of their neuraminidase (NA) activity. 35890-38-1 and 35890-39-2 are also in the experiment. Novel glycoconjugates with variations of terminally bound sialic acid mimicking the three main receptor types for influenza viruses were synthesized. These new substrates together with the lectin from Ricinus communis were used in a solid phase microtiter assay for the detection of NA specificity. Egg or MDCK isolated virus strains tended to exhibit highest NA activity against 3'sialyl-bound sialic acid whereas Vero isolated strains favored 6'sialyl-(N-acetyllactosamine)-bound sialic acid. Differences were more pronounced for influenza A than for influenza B strains. .