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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >A kinetically stable plant subtilase with unique peptide mass fingerprints and dimerization properties.
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A kinetically stable plant subtilase with unique peptide mass fingerprints and dimerization properties.

机译：具有独特的肽质量指纹图谱和二聚化特性的动力学稳定的植物枯草蛋白酶。

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摘要

Milin, a potent molluscicide from the latex of Euphorbia milii, holds promise in medicinal biochemistry. Electrophoresis, size exclusion chromatography, mass spectrometry and other biochemical characteristics identify milin as a homodimeric, plant subtilisin-like serine protease, the first of its kind. The subunits of milin are differentially glycosylated affecting dimer association, solubility and proteolytic activity. The dimeric dissociation is SDS-insensitive and strongly temperature dependent but does not appear to be linked by disulfide bridges. N-terminal sequence of acid hydrolyzed peptide fragments shows no homology to known serine protease. Peptide mass fingerprinting and de novo sequencing of the tryptic fragments also did not identify putative domains in the protein. Milin seems to be a novel plant enzyme with subunit association partly similar to human herpes virus serine proteases and partly to penicillin binding proteins. Its behaviour on SDS-PAGE gels and other properties is like kinetically stable a critical role in its physiological function and in controlling Schistosomiasis.
机译：Milin是一种来自大戟（Euphorbia milii）乳胶的有效杀软体动物剂，在药用生物化学中具有广阔的前景。电泳，尺寸排阻色谱法，质谱法和其他生化特征将milin鉴定为同源二聚体，是一种植物枯草杆菌蛋白酶样丝氨酸蛋白酶，是首例此类蛋白。米林的亚基被差异糖基化，影响二聚体缔合，溶解度和蛋白水解活性。二聚解离是对SDS不敏感的，并且与温度密切相关，但似乎不被二硫键连接。酸水解肽片段的N-末端序列与已知的丝氨酸蛋白酶没有同源性。胰蛋白酶片段的肽质量指纹图谱和从头测序也未鉴定出蛋白质中的推定结构域。 Milin似乎是一种具有亚基缔合的新型植物酶，部分与人疱疹病毒丝氨酸蛋白酶相似，而部分与青霉素结合蛋白相似。它在SDS-PAGE凝胶上的行为和其他特性就像动力学稳定一样，在其生理功能和控制血吸虫病中起着至关重要的作用。

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