title: The isolation and properties of a second glycoprotein (LGP-II) from the articular lubricating fraction from bovine synovial fluid.
abstract: A high-molecular-weight glycoprotein (LGP-I) was shown [Swann, Sotman, Dixon & Brooks (1977) Biochem. J. 161, 473--485] to be the major constituent in the articular lubricating fraction from bovine synovial fluid. In addition to the LGP-I component, a second glycoprotein (LGP-II) was also present. After fractionation of bovine synovial fluid by sequential sedimentation in CsCl density gradients, the LGP-I and LGP-II components were separated by gel-permeation chromatography. The LGP-II component was then purified by chromatography on DEAE Bio-Gel A and Bio-Gel P-150. The molecular weight of the LGP-II component was 48,800 calculated from sedimentation-equilibrium measurements. Amino acids represented 53% (w/w) and carbohydrate constituents 36% (w/w) of the molecule. Glutamic acid and lysine (144 and 100 residues/1000 residues) were the major amino acids. Glucosamine, mannose, galactose and N-acetylneuraminic acid [representing 8.0, 6.6, 9.5 and 11.9% (w/w) respectively] were the only carbohydrate constituents detected. Immunodiffusion analysis showed that LGP-II component did not form a detectable precipitin line with antiserum to bovine serum. It appears likely, therefore, that this glycoprotein is synthesized by the joint tissues and is not derived from serum.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002852:Chromatography, Ion Exchange; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D005779:Immunodiffusion; D008970:Molecular Weight; D013582:Synovial Fluid / Q000032:analysis*
chemical_list: D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins