Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual.

Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual.
复制标题

来自单个个体的多种形式的淀粉样蛋白相关血清蛋白 SAA 的氨基酸结构。

DOI:
10.1021/bi00405a044
复制
发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
Benson,MD
Benson,MD
中科院分区:
生物学3区
文献类型:
--
作者:
Dwulet,FE;Wallace,DK;Benson,MD

文献摘要

被引文献

相似文献

修订稿于 1987 年 10 月 30 日收到摘要:从单个个体的血浆脂蛋白部分中分离出多种形式的急性期血清蛋白 SAA。这些蛋白质形式通过尺寸排阻、离子交换和反相高压液相色谱进行纯化,然后对胰蛋白酶肽进行氨基酸序列分析。总共鉴定出三种不同的 104 个残基蛋白质。其中两种蛋白质的不同之处仅在于 71 位有精氨酸或组氨酸,而第三种蛋白质则有 7 个氨基酸差异。这些蛋白质均具有 103 个残基的伴随蛋白,其中氨基末端精氨酸已被去除。其中两个蛋白质序列与文献中报道的两个人类 SAA cDNA 结构相匹配。一个个体中存在三个独特的氨基酸序列证明人类中至少存在两个 SAA 基因。
Revised Manuscript Received October 30, 1987 abstract: Multiple forms of the acute-phase serum protein SAA were isolated from the lipoprotein fraction of plasma from a single individual. These protein forms were purified bysize-exclusion, ion-exchange, and reverse-phase high-pressure liquid chromatography, and then the tryptic peptides were subjected to amino acid sequence analysis. A total of three distinct 104-residue proteins were identified. Two of these proteins differed only by having either an arginine or a histidine at position 71 while the third protein had seven amino acid differences. Each of these proteins has a 103-residue companion protein where theamino-terminal arginine has been removed. Two of these protein sequences match the two human SAA cDNA structures reported in the literature. The presence of three unique amino acid sequences in one individual is proof that there must be a minimum of two genes for SAA inhumans.