TY - JOUR
T1 - Sulfobacins A and B, Novel von Willebrand Factor Receptor Antagonists
T2 - I. Production, Isolation, Characterization and Biological Activities
AU - Kamiyama, Tsutomu
AU - Umino, Takayuki
AU - Satoh, Tomoko
AU - Sawairi, Sayoko
AU - Shirane, Michiko
AU - Ohshima, Shoichi
AU - Yokose, Kazuteru
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1995
Y1 - 1995
N2 - Sulfobacins A and B, novel von Willebrand factor (vWF) receptor antagonists, have been isolated from the culture broth of Chryseobacterium sp. (Flavobacterium sp.)† NR 2993 by ethyl acetate extraction, and by Sephadex LH-20 and silica gel column chromatographies. The physico-chemical properties of the sulfobacins indicate that their structures are completely different from that of aurintricarboxylic acid, the one known vWF receptor antagonist. Sulfobacins A and B inhibit the binding of vWF to its receptor with IC50s of 0.47 and 2.2 μM, respectively. Sulfobacin A also inhibits ristocetin-induced agglutination in human platelets fixed with paraformaldehyde with an IC50 of 0.58 μM.
AB - Sulfobacins A and B, novel von Willebrand factor (vWF) receptor antagonists, have been isolated from the culture broth of Chryseobacterium sp. (Flavobacterium sp.)† NR 2993 by ethyl acetate extraction, and by Sephadex LH-20 and silica gel column chromatographies. The physico-chemical properties of the sulfobacins indicate that their structures are completely different from that of aurintricarboxylic acid, the one known vWF receptor antagonist. Sulfobacins A and B inhibit the binding of vWF to its receptor with IC50s of 0.47 and 2.2 μM, respectively. Sulfobacin A also inhibits ristocetin-induced agglutination in human platelets fixed with paraformaldehyde with an IC50 of 0.58 μM.
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U2 - 10.7164/antibiotics.48.924
DO - 10.7164/antibiotics.48.924
M3 - Article
C2 - 7592056
AN - SCOPUS:0028864772
SN - 0021-8820
VL - 48
SP - 924
EP - 928
JO - The Journal of Antibiotics
JF - The Journal of Antibiotics
IS - 9
ER -