Isolation and characterization of two glycoproteins from hyaline cartilage.
Two acidic glycoproteins of molecular mass 92 kDa and 56 kDa were purified from 4 M guanidine hydrochloride extracts of chick sternal cartilage, by density gradient centrifugation, ion-exchange chromatography, gel chromatography and SDS/PAGE. The glycoproteins differed in their amino acid and carbohydrate compositions. They were identified by the immunoblotting technique in extracts of chick articular cartilage from various sites and in extracts of cartilage from other species. The proteins are synthesized by the chondrocytes and show a partial cross-reactivity between their antisera.
Anagnostides
S T
ST
Department of Chemistry, University of Patras, Greece.
Aletras
A J
AJ
Lymberi
P
P
Tsiganos
C P
CP
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D002356:Cartilage / Q000737:chemistry*; D002499:Centrifugation, Density Gradient; D002645:Chickens; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000737:chemistry / Q000302:isolation & purification*; D015151:Immunoblotting; D008970:Molecular Weight; D009928:Organ Specificity; D013045:Species Specificity; D014574:Uronic Acids / Q000032:analysis
D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D014574:Uronic Acids