通过差异氚交换鉴定在β-内酰胺酶II中作为锌配体的组氨酸残基。
Identification of histidine residues that act as zinc ligands in beta-lactamase II by differential tritium exchange.
作者信息
Baldwin G S, Waley S G, Abraham E P
出版信息
Biochem J. 1979 Jun 1;179(3):459-63. doi: 10.1042/bj1790459.
Abstract
- Four histidine-containing peptides have been isolated from a tryptic digest of the Zn2+-requiring beta-lactamase II from Bacillus cereus. One of these peptides probably contains two histidine residues. 2. The presence of one equivalent of Zn2+ substantially decreases the rate of exchange of the C-2 proton in at least two and probably three of the histidine residues of these peptides for solvent 3H. 3. It is concluded that peptides containing at least two of the three histidine residues acting as Zn2+ ligands at the tighter Zn2+-binding site of beta-lactamase II have been identified.
摘要
- 从蜡样芽孢杆菌中需要锌离子的β-内酰胺酶II的胰蛋白酶消化物中分离出了四种含组氨酸的肽。其中一种肽可能含有两个组氨酸残基。2. 一当量锌离子的存在显著降低了这些肽中至少两个、可能三个组氨酸残基的C-2质子与溶剂3H的交换速率。3. 得出的结论是，已经鉴定出在β-内酰胺酶II的紧密锌离子结合位点上作为锌离子配体的三个组氨酸残基中至少含有两个组氨酸残基的肽。
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