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Nasir-ud-Din

Publications and source records attributed to Nasir-ud-Din.

28 records · Page 2Linked to original sources
PubMed1987

Structure of acidic oligosaccharides isolated from pronase-treated glycoprotein of bonnet-monkey (Macaca radiata) cervical mucus.

The major glycoprotein component of cervical mucus of bonnet monkey was treated with Pronase, and the enzyme-resistant glycoprotein purified by gel filtration on Sepharose 4B followed by DEAE-cellulose chromatography. Alkaline-borohydride cleavage of the carbohydrate chains gave a mixture of neutral and acidic oligosaccharides. Seven acidic oligosaccharides were characterized by chemical and enzymic procedures; their proposed structures are: alpha NeuAc(2----3)-[beta GalNAc(1----4)]beta Gal(1----4)GlcNAc(1----6)[alpha Fuc(1----2)beta Gal(1----3)]GalNAc-ol; alpha Fuc(1----2)beta Gal(1----3)/6)[alpha NeuAc(2----3)beta Gal(1----4)GlcNAc(1----3)/6)]GalNAc-ol; alpha GalNAc(1----3)beta Gal(1----3)[alpha NeuAc(2----3)beta Gal(1----4)GlcNAc(1----6)]GalNAc-ol; beta GlcNAc(1----3)[alpha Fuc(1----2)]beta Gal(1----3)[alpha NeuAc(2----6)]GalNAc-ol; beta Gal(1----3)-[alpha NeuAc(2----6)]GalNAc-ol; alpha NeuAc(2----6)GalNAc-ol; and beta Gal3SO3(1----4) GlcNAc(1----6)[alpha Fuc(1----2)beta Gal(1----3)]GalNAc-ol.

Animals↗
PubMed1985

The phosphate diester linkage of the peptidoglycan polysaccharide moieties of Micrococcus lysodeikticus cell wall.

The external polysaccharide is a major component of Micrococcus lysodeikticus cell wall and displays distinct composition. The complete structure of the external polysaccharide had been elucidated as a basis for investigation of the cell wall structure-function relation. However, the mode of attachment of the polysaccharide to the peptidoglycan through a phosphodiester was not clear due to limitations in structural and biosynthetic studies. The present study describes purification of a lysozyme-resistant nondialyzable high-molecular-weight fragment of cell wall and identifies the sugar, D-glucose, as the point of external polysaccharide attachment to the peptidoglycan through a phosphate diester. Kinetic studies for the acid-catalyzed release of external polysaccharide from the peptidoglycan were performed in parallel with synthetic [methyl-2-acetamido-3-O-(D-1-carboxyethyl)-2-deoxy-alpha-D- glucopyranoside-6-yl]-alpha-D-glucopyranosyl phosphate and alpha-D-glucopyranosyl phosphate and showed the presence of a phosphodiester linkage between external polysaccharide and peptidoglycan. In addition, type of phosphate residue and cross-linking between muramic acid and protein part have been determined.

Amino Acids↗
PubMed1983

Bonnet monkey cervical mucus glycoproteins. Study of the minor glycoprotein components of periovulatory phase mucus.

Two glycoproteins present in small quantities, in addition to a main glycoprotein, were isolated from the periovulatory phase mucus. The glycoproteins, obtained in minute amounts, showed distinct variations in the relative proportions of sugar residues. The results of analytical as well as chemical studies suggest the existence of two distinct molecular species differing in structure. The main component of the minor glycoproteins, Fraction A, Characterized by Smith degradation and by subsequent methylation and inhibition of hemagglutination, bears similarities to the periovulatory phase main glycoprotein. The other component, Fraction B, characterized by Smith degradation followed by inhibition of hemagglutination, shows structural resemblance to the premenstrual phase glycoprotein.

Amino Acids↗
PubMed1981

Studies on bonnet monkey cervical mucus. The effect of proteases on mucus glycoproteins of Macaca radiata.

The influence of proteinases on monkey cervical glycoproteins was investigated to assess their effect on cervical mucus and, thereby, on sperm penetration. The major component of periovulatory cervical mucus, a high molecular weight glycoprotein, was treated with Pronase, trypsin, chymotrypsin, papain, and bovine seminal peptidase, and the enzyme-resistant glycoprotein was purified by gel filtration on Sepharose 2B. A macromolecular component in high yield was recovered containing carbohydrate and protein moieties. Asialoglycoprotein, on treatment with Pronase, trypsin, and bovine seminal peptidase released more than one glycoprotein fragment. The carbohydrate and amino acid components of the native and degraded glycoproteins were similar in composition with variations in proportions. The structure of the carbohydrate-rich, pronase-resistant glycoprotein, further purified on Sepharose 2B, was examined. Sequential Smith degradation and methylation of the degraded glycoprotein fragment established a structure that shows some differences to that of the native glycoprotein. The influence of proteinases on cervical-mucus glycoproteins and a possible mechanism of sperm penetration through Pronase-treated glycoproteins is discussed.

Animals↗