Conformational dynamics of porcine pancreatic colipase: A 360 MHz proton nuclear magnetic resonance study
Conformational dynamics of porcine pancreatic colipase: A 360 MHz proton nuclear magnetic resonance study
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猪胰辅脂肪酶的构象动力学：360 MHz 质子核磁共振研究
DOI：
10.1016/0014-5793(76)80674-6
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发表时间：
1976
期刊：
影响因子：
3.5
通讯作者：
P. Cozzone
中科院分区：
文献类型：
--
作者：
P. Cozzone
本研究致力于辅脂酶II，猪胰辅脂酶的两种主要分子形式之一[1，2]。这种小蛋白的分子量为8700，由84个氨基酸残基的单链多肽组成[3，4]。其氨基酸序列已被确定[3]，对应于由5个二硫键维持的相当紧凑的结构[4]。辅脂酶的生物学作用非常重要，因为它在体内作为辅助因子，阻止生理浓度的胆汁盐对饮食甘油三酯十二指肠内脂解的抑制作用[1，5，6]。为了解释辅脂酶的生理作用，最近在各种实验条件下研究了辅脂酶、脂肪酶和胆汁盐的二元和三元缔合[7-13]。通常，辅脂酶已显示结合化学计量量的胆汁盐胶束，并形成胰脂肪酶可以识别的二元复合物。这些结合和识别过程可能涉及在辅脂酶分子上产生和/或揭示适当位点的特定构象变化[II]。
The present study is devoted to colipase II, one of the two main molecular forms of porcine pancreatic colipase [1, 2]. This small protein has a molecular weight of 8700 and consists of a single polypeptide chain of 84 amino acid residues [3, 4]. Its amino acid sequence has been determined [3] and corresponds to a rather compact structure maintained by 5 disulfide bridges [4]. The biological role of colipase is of great importance since it acts in vivo as a cofactor preventing the inhibitory effect of physiological concentrations of bile salts on the intraduodenal lipolysis of dietary triglycerides [1, 5, 6]. In an attempt to explain the physiological effect of colipase, binary and ternary associations of colipase, lipase and bile salts have been recently investigated under a variety of experimental conditions [7-13]. Typically, colipase has been shown to bind stoichiometrical amounts of bile salt micelles and to form a binary complex that pancreatic lipase can in turn recognize. It is likely that these binding and recognition processes involve specific conformational changes creating and/or unveiling appropriate sites on the colipase molecule [ll].