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Ocellatusin is a new RGD-containing short monomeric disintegrin. It is a better inhibitor of α 5 β 1 integrin and a more potent inducer of the expression of a ligand-induced binding site epitope on β 1 integrin subunit than echistatin. In further contrast to echistatin, ocellatusin has a direct chemotactic stimulus on human neutrophils in vitro. The distinct effects of these...
The disulphide bond pattern of the long disintegrin bitistatin (83 amino acids, 14 cysteines) was established using structural information gathered by amino acid analysis, N-terminal sequencing, and molecular mass determination of fragments isolated by reversed-phase HPLC after polypeptide degradation with trypsin and oxalic acid. A computer program was used to calculate all possible combinations...
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