Shinohara C, Hasumi K, Hatsumi W, Endo A
Department of Applied Biological Science, Tokyo Noko University, Japan.
J Antibiot (Tokyo). 1996 Oct;49(10):961-6. doi: 10.7164/antibiotics.49.961.
A novel triprenyl phenol, designated staplabin, has been isolated from a culture of Stachybotrys microspora IFO 30018 by solvent extraction and successive chromatographic fractionation using silica gel, Sephadex LH-20 and silica ODS columns. By a combination of spectroscopic analyses, the structure of staplabin is proposed to be 5-(2-(5,7-dihydroxy-8-methyl-8-(4,8-dimethyl-3,7-nonadienyl)-3-oxo -7, 8-dihydro-6H-pyrano[2,3-e][1,3]dihydroisoindolyl)pentanoic acid. Staplabin stimulated the binding of plasminogen, the zymogen of the fibrinolytic serine protease plasmin, to both fibrin and U937 cells. Binding was elevated 2-fold at a concentration of 0.3 approximately 0.5 mM.
一种名为葡萄穗霉毒素的新型三萜烯基苯酚，已通过溶剂萃取以及使用硅胶、葡聚糖凝胶LH - 20和硅胶ODS柱的连续色谱分离，从微小葡萄穗霉IFO 30018的培养物中分离出来。通过光谱分析的组合，葡萄穗霉毒素的结构被推测为5 - (2 - (5,7 - 二羟基 - 8 - 甲基 - 8 - (4,8 - 二甲基 - 3,7 - 壬二烯基) - 3 - 氧代 - 7,8 - 二氢 - 6H - 吡喃并[2,3 - e][1,3]二氢异吲哚基)戊酸。葡萄穗霉毒素刺激纤溶酶原（纤维蛋白溶解丝氨酸蛋白酶纤溶酶的酶原）与纤维蛋白和U937细胞的结合。在浓度约为0.3至0.5 mM时，结合增加了2倍。
