FEBS Letters | |
Specific inhibition of binding of antistasin and [A103,106,108] antistasin 93–119 to sulfatide (Gal(3‐SO4)β1‐1Cer) by glycosaminoglycans | |
Manley, George D.1  Brankamp, Robert G.1  Cardin, Alan D.1  Krstenansky, John L.2  Owen, Thomas J.1  | |
[1] Marion Merrell Dow Research Institute, 2110 East Galbraith Rd, Cincinnati, OH 45215, USA;Syntex Research, 3401 Hillview Ave., Palo Alto, CA 94303, USA | |
关键词: Antistasin; Ghilanten; Haementeria; Sulfatide; Glycosaminoglycans; Leech; | |
DOI : 10.1016/0014-5793(92)80366-O | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 [A103,106,108] 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.
【 授权许可】
Unknown
【 预 览 】
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