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Specific inhibition of binding of antistasin and [A 103,106,108 ] antistasin 93–119 to sulfatide (Gal(3‐SO4)β1‐1Cer) by glycosaminoglycans
Author(s) -
Brankamp Robert G.,
Manley George D.,
Owen Thomas J.,
Krstenansky John L.,
Cardin Alan D.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80366-o
Subject(s) - dermatan sulfate , glycosaminoglycan , sulfation , chemistry , heparin , chondroitin sulfate , chondroitin , biochemistry , plasma protein binding , binding site , leech , sulfate , stereochemistry , organic chemistry , world wide web , computer science
Leech‐derived antistasin is a potent anticoagulant and antimetastatic protein that binds sulfatide (Gal(3‐SO4)β1‐1Cer)and sulfated polysaccharides. In this study, the synthetic fragment [A 103,106,108 ] antistasin 93–119, which corresponds to the carboxyl terminus, showed specific and saturable binding to sulfatide. Binding was competitively blocked by glycosaminoglycans (GAGs) in the order: dextran sulfate 5000 ≅ dextran sulfate 500 0OO > heparin > dermatan sulfate ⪢ chondroitin sulfates A and C. This rank order of inhibitory potency was identical to that observed with whole antistasin. We suggest that residues 93–119 of antistasin represent a critical domain for binding GAGs and sulfated glycolipids.