转谷氨酰胺酶催化牛β-乳球蛋白C末端区域谷氨酰胺侧链的修饰。
Transglutaminase catalyses the modification of glutamine side chains in the C-terminal region of bovine beta-lactoglobulin.
作者信息
Coussons P J, Price N C, Kelly S M, Smith B, Sawyer L
机构信息
Department of Biological and Molecular Sciences, University of Stirling, Scotland, U.K.
出版信息
Biochem J. 1992 May 1;283 ( Pt 3)(Pt 3):803-6. doi: 10.1042/bj2830803.
The transglutaminase-catalysed incorporation of primary amines (putrescine and monodansylcadaverine) into bovine beta-lactoglobulin has been studied. In the presence of 1 mM-dithiothreitol between 1 and 2 mol of amine can be incorporated per mol of beta-lactoglobulin subunit. There is very little incorporation of amines in the absence of reducing agent. By isolating and sequencing the modified peptides, the sites of modification have been identified as Gln-159 (preferred) and Gln-155. C.d. has been used to study the structure of beta-lactoglobulin over a range of pH values and in the presence or absence of dithiothreitol. The results are discussed in terms of the X-ray-crystallographically determined structure of beta-lactoglobulin.
已对转谷氨酰胺酶催化伯胺（腐胺和单丹磺酰尸胺）掺入牛β-乳球蛋白的过程进行了研究。在1 mM二硫苏糖醇存在的情况下，每摩尔β-乳球蛋白亚基可掺入1至2摩尔胺。在没有还原剂的情况下，胺的掺入量非常少。通过分离和测序修饰后的肽段，已确定修饰位点为Gln-159（优先）和Gln-155。圆二色光谱已用于研究在一系列pH值以及存在或不存在二硫苏糖醇的情况下β-乳球蛋白的结构。根据X射线晶体学确定的β-乳球蛋白结构对结果进行了讨论。
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