Seo Y, Nakayama T, Takahama K
Department of Legal Medicine, Miyazaki Medical College, Japan.
Nihon Hoigaku Zasshi. 1993 Feb;47(1):1-5.
We have purified a liver-specific antigen (LSA) from human liver by using immunoaffinity chromatography followed by other procedures and examined its biochemical properties. Amino acid analysis of the purified LSA revealed that the sum of acidic amino acids was probably higher than that of basic amino acids; this agrees with its pI of 5.8-5.9. The protein had also relatively large amount of Pro and the NH2-terminal amino acid sequence from 2nd to 8th residues was determined to be Pro-Pro-Ser-Pro-Pro-Val-Val. A computer search showed that the human LSA has no significant homology to any other proteins available from sequence databases. These findings, together with those reported previously, suggest that the human LSA will be useful as a powerful marker for detecting liver injury.
我们通过免疫亲和层析及其他方法从人肝脏中纯化了一种肝脏特异性抗原（LSA），并检测了其生化特性。对纯化后的LSA进行氨基酸分析发现，酸性氨基酸的总和可能高于碱性氨基酸；这与其5.8 - 5.9的pI相符。该蛋白质还含有相对大量的脯氨酸，且第2至8个残基的氨基末端氨基酸序列被确定为脯氨酸-脯氨酸-丝氨酸-脯氨酸-脯氨酸-缬氨酸-缬氨酸。计算机检索表明，人LSA与序列数据库中任何其他可用蛋白质均无显著同源性。这些发现与先前报道的结果一起表明，人LSA将作为检测肝损伤的有力标志物发挥作用。
