A high-molecular-weight (greater than 8.10(5)) non-collagenous glycoprotein is synthesized by bovine cartilage in vitro.
A high-molecular-weight (greater than 8.10(5)) glycoprotein was detected in [3H]glucosamine-labeled bovine cartilage. Extraction with varying amounts of guanidinium chloride showed that the molecule was not tightly bound to other matrix substances. Enzyme digestions identified the molecule as a non-collagenous glycoprotein. This glycoprotein constituted 10-20% of the [3H]glucosamine-labeled macromolecular material that was released into culture medium on the first day after labeling. The 3H-labeled glycoprotein was purified by anion-exchange chromatography, CsCl gradient centrifugation and gel filtration. The purified glycoprotein appeared on an SDS-polyacrylamide gel as one slightly polydisperse band, which could not be reduced by beta-mercaptoethanol.
Visser
N A
NA
Jan van Breemen Institute for Rheumatology and Rehabilitation, Amsterdam, The Netherlands.
Brand
H S
HS
Vankampen
G P
GP
Vandestadt
R J
RJ
Vanderkorst
J K
JK
D000818:Animals; D002358:Cartilage, Articular / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D002478:Cells, Cultured; D005260:Female; D006023:Glycoproteins / Q000096:biosynthesis* / Q000302:isolation & purification; D006821:Hyaluronoglucosaminidase; D006868:Hydrolysis; D003012:Microbial Collagenase; D008970:Molecular Weight; D014316:Tritium
D006023:Glycoproteins; D014316:Tritium; D006821:Hyaluronoglucosaminidase; D003012:Microbial Collagenase