肺半乳糖凝集素和纤连蛋白精氨酸残基的化学修饰。对成纤维细胞结合的影响。
Chemical modification of arginine residues of lung galaptin and fibronectin. Effects on fibroblast binding.
作者信息
Powell J T
出版信息
Biochem J. 1985 Dec 15;232(3):919-22. doi: 10.1042/bj2320919.
Abstract
Lung galaptin bound to lung fibroblasts with a Kd of 190 nM, and this binding could be inhibited by 20 mM-lactose. Selective modifications of the arginine residues of galaptin with cyclohexane-1,2-dione did not change its lectin activity or its binding to fibroblasts. By contrast, modification of the arginine residues of plasma fibronectin resulted in a marked diminution of protein-fibroblast binding. Selective modification of arginine residues may provide a useful probe for -Arg-Gly-Asp-Xaa cell-binding sequences of proteins.
摘要
肺半乳糖凝集素以190 nM的解离常数（Kd）与肺成纤维细胞结合，且这种结合可被20 mM乳糖抑制。用环己烷-1,2-二酮对半乳糖凝集素的精氨酸残基进行选择性修饰，不会改变其凝集素活性或与成纤维细胞的结合。相比之下，对血浆纤连蛋白的精氨酸残基进行修饰会导致蛋白质与成纤维细胞的结合显著减少。精氨酸残基的选择性修饰可能为蛋白质的-Arg-Gly-Asp-Xaa细胞结合序列提供一种有用的探针。
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