Fractionation of Glycoprotein Components of the Reduced Alkylated Renal Glomerular Basement Membrane

摘要: Abstract The soluble glycoprotein components of the S-carboxy-methylated glomerular basement membrane were fractionated by gel filtration in sodium dodecyl sulfate on agarose columns varying porosity and DEAE-cellulose chromatography urea. By such techniques, these components, which represented 70 to 80% total ranged molecular weight from 30,000 greater than 700,000, resolved into fractions differing markedly their amino acid sugar composition. Some contained large amounts hydroxyproline, glycine, hydroxylysine, while others had fewer acids characteristic collagen richer as aspartic acid, serine, threonine, tyrosine, lysine, histidine, S-carboxymethyl-cysteine. with more collagen-like composition a higher number hydroxylysine-linked glucosylgalactose disaccharide units did polar nature, many 35 per 1000 occurring former few 2 latter. heteropolysaccharide (consisting sialic fucose, galactose, mannose, hexosamines) evenly distributed, ranging 1 4 somewhat content being present fractions. Both occurred spanning wide range. former, however, tended be predominantly associated high material (over 100,000). These results are believed consistent occurrence both chains, containing di- latter having only polysaccharides. Although disulfide bonds appear serve major crosslink between peptide chains this membrane, NH2-terminal analyses suggested that other yet undefined cross-links may exist.