Leong T Y, Schweiger H G
Eur J Biochem. 1979 Jul;98(1):187-94. doi: 10.1111/j.1432-1033.1979.tb13176.x.
A polypeptide (polypeptide P39), which is presumed to involved in the photosynthetic circadian rhythm in the green alga Acetabularia, was purified from the EDTA-insoluble chloroplast membrane fraction by means of preparative dodecylsulfate gel electrophoresis and then partially characterized. The purity of the isolated polypeptide P39 was confirmed by a further electrophoresis on an analytical dodecylsulfate gel and further elucidated by amino-terminal analysis which shows that glycine is the only amino-terminal amino acid of the purified polypeptide material. The molecular weight of the polypeptide P39 was found to be about 39,000 on analytical gel electrophoresis and the value was further supported by those obtained from amino acid composition and peptide mapping. The amino acid composition of polypeptide P39 showed that the proportion of intermediate amino acid groups is high while the proportion of hydrophilic amino acid groups is well balanced by that of hydrophobic amino acid groups, a property characteristic of membrane proteins.
一种被认为与绿藻伞藻光合昼夜节律有关的多肽（多肽P39），通过制备型十二烷基硫酸钠凝胶电泳从EDTA不溶性叶绿体膜组分中纯化出来，然后进行了部分特性鉴定。通过在分析型十二烷基硫酸钠凝胶上进一步电泳确认了分离出的多肽P39的纯度，并通过氨基末端分析进一步阐明，该分析表明甘氨酸是纯化多肽物质唯一的氨基末端氨基酸。在分析型凝胶电泳上发现多肽P39的分子量约为39,000，氨基酸组成和肽图谱分析得到的值进一步支持了该结果。多肽P39的氨基酸组成表明，中间氨基酸基团的比例较高，而亲水氨基酸基团的比例与疏水氨基酸基团的比例保持良好平衡，这是膜蛋白的一个特性。
