Abstract
A single type-II domain has been isolated by limited proteolysis of the collagen-binding bovine seminal fluid protein, PDC-109. The 45-residue fragment corresponding to the second type-II domain of the parent molecule was found to have retained affinity for immobilized collagen, indicating that this minidomain carries critical regions of the collagen-binding site. Studies on various fragments of fibronectin have also implicated the two type-II units of this molecule in collagen-binding. In the present work we have found that type-II domains of human fibronectin, expressed in Escherichia coli as beta-galactosidase fusion proteins, bind specifically to immobilized collagen.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Cattle
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Chromatography, Affinity
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Cloning, Molecular
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Collagen / metabolism*
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Fibronectins / genetics
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Fibronectins / isolation & purification
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Fibronectins / metabolism*
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Male
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Molecular Sequence Data
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Plasmids
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Prostatic Secretory Proteins*
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Protein Conformation
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Proteins / isolation & purification
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Proteins / metabolism*
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Restriction Mapping
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Semen / metabolism
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Seminal Plasma Proteins
Substances
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Fibronectins
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Prostatic Secretory Proteins
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Proteins
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Recombinant Fusion Proteins
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Seminal Plasma Proteins
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beta-microseminoprotein
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Collagen