人脑S100蛋白组分的特性：S100β的氨基酸序列

Characterization of human brain S100 protein fraction: amino acid sequence of S100 beta.

作者信息

Jensen R, Marshak D R, Anderson C, Lukas T J, Watterson D M

出版信息

J Neurochem. 1985 Sep;45(3):700-5. doi: 10.1111/j.1471-4159.1985.tb04048.x.

DOI:10.1111/j.1471-4159.1985.tb04048.x

Abstract

Two major components of human brain S100 fraction were purified by HPLC and an amino acid sequence was elucidated for the S100 beta component. Human S100 proteins showed absorption spectra and amino acid compositions similar to S100 alpha and S100 beta from bovine brain. However, the relative amounts of the human proteins were 4% S100 alpha and 96% S100 beta by weight, while the bovine protein distribution was 47% S100 alpha and 53% S100 beta by weight. An amino acid sequence of human S100 beta was established by analysis of overlapping fragments generated by cyanogen bromide and trypsin cleavage. Three amino acid sequence differences between the human and bovine S100 beta were found at residues 7, 62, and 80. These differences were chemically conservative and compatible with minimum single base changes in the codon structures. These results document that S100 beta is a conserved protein among mammals and provide the necessary foundation for current clinical studies.

摘要

通过高效液相色谱法纯化了人脑海马体S100组分的两个主要成分，并阐明了S100β组分的氨基酸序列。人S100蛋白的吸收光谱和氨基酸组成与牛脑海马体中的S100α和S100β相似。然而，按重量计算，人S100蛋白中S100α的相对含量为4%，S100β为96%，而牛S100蛋白的分布是S100α为47%，S100β为53%。通过分析由溴化氰和胰蛋白酶切割产生的重叠片段，确定了人S100β的氨基酸序列。在人S100β和牛S100β之间，在第7、62和80位残基处发现了三个氨基酸序列差异。这些差异在化学上是保守的，并且与密码子结构中最小的单碱基变化相一致。这些结果证明S100β是哺乳动物中一种保守的蛋白质，并为当前的临床研究提供了必要的基础。