首页> 美国卫生研究院文献>Biochemical Journal >Evidence for an increase in positive surface charge and an increase in susceptibility to trypsin of Sarcophaga lectin (from the flesh fly Sarcophaga peregrina) on its interaction with galactose a hapten sugar of the lectin.
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Evidence for an increase in positive surface charge and an increase in susceptibility to trypsin of Sarcophaga lectin (from the flesh fly Sarcophaga peregrina) on its interaction with galactose a hapten sugar of the lectin.

机译:有证据表明与半乳糖(一种凝集素的半抗原)相互作用时石蜡凝集素(来自果蝇Sarcophaga peregrina)的表面正电荷增加对胰蛋白酶的敏感性增加。

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摘要

When Sarcophaga lectin (from the flesh fly, Sarcophaga peregrina), an insect humoral lectin, was eluted from a column of DEAE-cellulose in the presence of galactose (a hapten sugar of this lectin), it emerged at a lower salt concentration than when galactose was absent. In the presence of galactose the lectin was, in addition, more susceptible to trypsin digestion. The lectin was found to have an affinity for basic proteins such as histone H3 and sarcotoxin IA, but this property was lost in the presence of galactose. These results suggested that the lectin changes its conformation on interaction with galactose. This change is suggested to result in the exposure of some hidden lysine and/or arginine residues.
机译:当在半乳糖(该凝集素的半抗原糖)存在下,从DEAE-纤维素柱上洗脱昆虫体液性凝集素Sarcophaga lectin(来自果蝇Sarcophaga peregrina)时,其盐浓度低于半乳糖不存在。另外,在半乳糖的存在下,凝集素更容易受到胰蛋白酶消化。发现该凝集素对碱性蛋白(例如组蛋白H3和肌毒素IA)具有亲和力,但是在半乳糖存在的情况下丧失了该特性。这些结果表明,凝集素在与半乳糖相互作用时改变其构象。建议此更改导致暴露一些隐藏的赖氨酸和/或精氨酸残基。

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