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Isolation and characterization of two glycoproteins from hyaline cartilage
Author(s) -
ANAGNOSTIDES Stavros T.,
ALETRAS Alexis J.,
LYMBERI Peggy,
TSIGANOS Constantine P.
Publication year - 1990
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1990.tb19416.x
Subject(s) - glycoprotein , cartilage , molecular mass , antiserum , chemistry , ion chromatography , hyaline cartilage , guanidine , biochemistry , chromatography , centrifugation , differential centrifugation , biology , antibody , anatomy , articular cartilage , medicine , osteoarthritis , pathology , immunology , enzyme , alternative medicine
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.

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