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J. Biol. Chem., Vol. 265, Issue 14, 8297-8303, 05, 1990
JL Funderburgh and GW Conrad
Bovine corneal keratan sulfate proteoglycan was found to contain three
major protein components. Two proteins (37 and 25 kDa) were released from
the proteoglycan by endo-beta-galactosidase, N-glycanase, or chemical
deglycosylation. A smaller protein (20 kDa), not covalently linked to
keratan sulfate, co-purified with the proteoglycan by conventional and high
performance ion exchange chromatography, by ethanol precipitation, and by
affinity purification on columns of monoclonal antibody to keratan sulfate,
but could be separated from the proteoglycan by gel filtration
chromatography in dissociative agents. The three proteins produced
different fragmentation patterns on sodium dodecyl sulfate-polyacrylamide
gel electrophoresis after digestion with V8 protease, and each had unique
two-dimensional tryptic peptide maps. The N-terminal amino acid sequence of
the core proteins differed. In addition, the proteoglycans containing these
proteins differed in molecular size, suggesting different levels of
glycosylation of the two core proteins. Similarity of the core proteins was
suggested by similar amino acid composition, similarities in tryptic maps,
and antigenic cross-reactivity. Corneal keratan sulfate proteoglycan,
therefore, seems to occur in two different, but related, forms whose core
proteins may represent members of a homologous family.
Isoforms of corneal keratan sulfate proteoglycan
Division of Biology, Kansas State University, Manhattan 66506.
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