Prevention of thermal inactivation and aggregation of lysozyme by polyamines
Prevention of thermal inactivation and aggregation of lysozyme by polyamines
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DOI：
10.1046/j.1432-1033.2003.03850.x
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发表时间：
2003-11-01
期刊：
影响因子：
--
通讯作者：
Takagi, M
中科院分区：
文献类型：
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作者：
Kudou, M;Shiraki, K;Takagi, M
蛋白质在高温下倾向于形成无活性的聚集体。我们发现，多胺，它有一个相对简单的结构作为寡酰胺，有效地防止热灭活和聚集的鸡蛋溶菌酶。在添加剂存在下，包括精氨酸和胍（100 mM），在磷酸钠缓冲液（pH 6.5）中，超过30%的0.2 mg.mL（-1）溶菌酶通过热处理（98 ℃，30 min）形成不溶性聚集体。然而，在存在50 mM精胺或亚精胺的情况下，在相同的热处理后未观察到聚集体。这种热处理后溶菌酶的残余活性很低（
Proteins tend to form inactive aggregates at high temperatures. We show that polyamines, which have a relatively simple structure as oligoamids, effectively prevent thermal inactivation and aggregation of hen egg lysozyme. In the presence of additives, including arginine and guanidine (100 mM), more than 30% of 0.2 mg.mL(-1) lysozyme in sodium phosphate buffer (pH 6.5) formed insoluble aggregates by heat treatment (98degreesC for 30 min). However, in the presence of 50 mM spermine or spermidine, no aggregates were observed after the same heat treatment. The residual activity of lysozyme after this heat treatment was very low (