Detail of "2492-87-7"

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Acquired B antigen: further studies using synthetic oligosaccharides

Acquired B antigen: further studies using synthetic oligosaccharides. Rahuel, C.; Lubineau, A.; David, S.; Salmon, C.; Cartron, J.Chemicals with cas numbers 2492-87-7 and 76888-07-8 also play role. P. (Lab. Biochim. Genet., INSERM, Fr.). Rev. Fr. Transfus. Immuno-Hematol., 26(4), 347-58 (English) 1983. CODEN: RFTID6. ISSN: 0338-4535. DOCUMENT TYPE: Journal CA Section: 15 (Immunochemistry) The reactivity of acquired-B red cells with various antisera was investigated by agglutination inhibition assays using 4 trisaccharides. Two of these had the structure GalNAca 1-3 (LFuca 1-2) Gal and Gala 1-3 (LFuca 1-2) Gal which are characteristic of the A and B determinants, resp. The 2 other sugars, denoted B-OAc and B-NH2, are derivs. of the B-trisaccharide by substitution of the hydroxyl group on C-2 of the a-galactose residue with the O-acetyl group (B-OAc) or the amino group (B-NH2), resp. Both B and B-NH2 trisaccharides inhibited strongly the agglutination of acquired B red cells by the anti-B reagents, whereas sera contg. anti-acquired B agglutinins were specifically inhibited by B-NH2, but not by the A, B, or B-OAc structures. Addnl., the agglutination of Tk-activated erythrocytes by the Bandeiraea simplicifalia II lectin was specifically inhibited by N-acetylglucosamine, but not by B, B-OAc, or B-NH2 structures. These results and the observation that anti-acquired B agglutinins cannot be adsorbed on Tk red cells suggest that (i) the B-like and the acquired-B determinants share a common structure best represented by B-NH2 and (ii) Tk and acquired-B antigens are not identical. .

Properties of b-glucosidase from pollen and carpels of Lathyrus odoratus L

Properties of b-glucosidase from pollen and carpels of Lathyrus odoratus L. Setia, Neelam; Malik, C. P.In this study， 9001-22-3 and 2492-87-7 are also used. (Coll. Basic Sci. Humanit., Punjab Agric. Univ., Ludhiana 141 004, India). J. Palynol., 18-19(1-2), 121-6 (English) 1983. CODEN: JPLYAR. ISSN: 0022-3379. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The activity of b-glucosidase (I) in ungerminated pollen and carpels is estd. in L. odoratus. The kinetic properties of I from pollen washing and cytoplasmic exts. of pollen and carpels were also studied in terms of the Km, inhibition by saccharides, pH, and thermostability. The Km of I from pollen washing (extracellular enzyme) and cytoplasmic enzymes from pollen and carpels were the same. I from these sources differed in thermostability, but had similar pH optima. .