DIRECT EVIDENCE FOR THE INVOLVEMENT OF DOMAIN-III IN THE N-F TRANSITION OF BOVINE SERUM-ALBUMIN
DIRECT EVIDENCE FOR THE INVOLVEMENT OF DOMAIN-III IN THE N-F TRANSITION OF BOVINE SERUM-ALBUMIN
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DOI：
10.1042/bj2360307
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发表时间：
1986-05-15
影响因子：
4.1
通讯作者：
KHAN, MY
中科院分区：
文献类型：
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作者：
KHAN, MY
分离了含有蛋白质序列的残基377-582的牛血清白蛋白的结构域III，并研究了其在酸性溶液中的行为。发现该片段在已知引起血清白蛋白中N-F转变的pH 3.5-4.5范围内经历结构转变。另一方面，缺乏结构域III的白蛋白片段不能表现出这样的转变。这些结果与N-F转换涉及结构域III与白蛋白分子的其余部分分离以及结构域III的亚结构域彼此分离的机制一致。结构转变开始于约pH 4.3，并在pH 3.5完成。
The domain III of bovine serum albumin containing residues 377-582 of the protein sequence was isolated and its behaviour in acid solution was studied. The fragment was found to undergo structural transformations over the pH range 3.5-4.5 known to cause N-F transition in serum albumin. On the other hand, an albumin fragment that was devoid of domain III was unable to exhibit such a transition. These results were consistent with a mechanism where N-F transition involves the separation of domain III from the rest of the albumin molecule as well as the separation of the subdomains of domain III from each other. The structural transitions starts at about pH 4.3 and is completed at pH 3.5.