vitronectin PAI-1结合位点的识别。
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西于尔扎多蒂啊,Wiman B
vitronectin PAI-1结合位点的识别。
Biochim Biophys学报。1994年9月21日,1208 (1):104 - 10。
- PubMed ID
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7522053 (在PubMed]
- 文摘
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活跃PAI-1(纤溶酶原激活物抑制剂1)必将vitronectin在血浆和细胞外基质。在这项研究中,我们旨在识别PAI-1 vitronectin结合位点,目前这是一个争议的问题。Vitronectin与胰蛋白酶裂解和碎片检测抑制性影响PAI-1 / Vitronectin交互使用vitronectin-coated微量滴定板。完整vitronectin vitronectin的胰蛋白酶的消化都引起PAI-1绑定的浓度减少50% 2 nmol /我。在交联葡聚糖凝胶过滤G-50超细的胰蛋白酶的肽抑制活动主峰之一。Kav的洗脱体积是0.55指示(a)中型肽(年代)。肽是通过反相高效液相色谱进一步纯化。结构分析表明,它构成了45 NH2-terminal vitronectin氨基酸残基。的NH2-terminal vitronectin肽引起的降低50% PAI-1绑定到vitronectin-coated微量滴定板的浓度约13 nmol / l。因此,肽是一种比完整vitronectin少有效的在这方面。 Reduced and S-carboxymethylated peptide had no effect on the interaction. The NH2-terminal vitronectin fragment increased the stability of active PAI-1 by about 60%, which is a little less than with intact vitronectin. The peptide also prevented PAI-1 from oxidation with chloramine T. The half-life was prolonged about 4-fold as compared to about 30-fold with intact vitronectin.