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通过序列分析对实验诱导的豚鼠淀粉样纤维进行分离和鉴定。

Isolation and identification by sequence analysis of experimentally induced guinea pig amyloid fibrils.

作者信息

Skinner M, Cathcart E S, Cohen A S, Benson M D

出版信息

J Exp Med. 1974 Sep 1;140(3):871-6. doi: 10.1084/jem.140.3.871.

Abstract

Amyloidosis was produced experimentally in guinea pigs by multiple casein injections. Amyloid fibrils were isolated and fractionated and a protein obtained that had an amino acid composition comparable with A protein, a unique nonimmunoglobulin constituent of secondary amyloid deposits. N-terminal sequence analysis demonstrated a sequence homologous with that of A proteins from human and monkey preparations but preceded by a 5-residue peptide which had an N-terminal histidine. A definite species specificity in A protein from human and guinea pig was identified on immunologic analysis.

摘要

通过多次注射酪蛋白在豚鼠中实验性地诱导出淀粉样变性。分离并分级淀粉样纤维,得到一种蛋白质,其氨基酸组成与A蛋白相当,A蛋白是继发性淀粉样沉积物中一种独特的非免疫球蛋白成分。N端序列分析表明,该序列与来自人和猴制剂的A蛋白序列同源,但前面有一个5个残基的肽段,其N端为组氨酸。免疫分析确定了人和豚鼠A蛋白之间存在明确的物种特异性。

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