血小板衍生生长因子 - BB（PDGF - BB）以及在酿酒酵母中表达的PDGF - BB蛋白酶抗性突变体的结构与构象表征。
Characterization of the structure and conformation of platelet-derived growth factor-BB (PDGF-BB) and proteinase-resistant mutants of PDGF-BB expressed in Saccharomyces cerevisiae.
作者信息
Craig S, Clements J M, Cook A L, Dryden D T, Green D R, Heremans K, Kirwin P M, Price M J, Fallon A
机构信息
British Bio-technology Ltd., Cowley, Oxford, U.K.
出版信息
Biochem J. 1992 Jan 1;281 ( Pt 1)(Pt 1):67-72. doi: 10.1042/bj2810067.
A detailed biophysical study of the secondary and tertiary structures of recombinant platelet-derived growth factor (PDGF)-BB produced in yeast has been carried out. The secondary structure of the molecule is composed of 54% beta-sheet with less than 5% ordered helix. The single tryptophan residue has been shown to be solvent-accessible; however, the ability of the side chain to rotate is severely restricted. The fluorescence emission is quenched at pH 7.0 and in the presence of high salt, but dequenched by titration to lower pH with a pK of 5.8. Two proteinase-resistant mutants of PDGF [( Ser28]- and [Pro32]-PDGF-BB) have also been characterized and shown to have secondary and tertiary structures indistinguishable from wild-type PDGF-BB. These are, therefore, suitable stable background molecules in which to carry out structure-activity-relationship studies on PDGF-BB.
对酵母中产生的重组血小板衍生生长因子（PDGF）-BB的二级和三级结构进行了详细的生物物理研究。该分子的二级结构由54%的β-折叠组成，有序螺旋结构少于5%。已证明单个色氨酸残基可与溶剂接触；然而，其侧链的旋转能力受到严重限制。在pH 7.0和高盐存在下，荧光发射被淬灭，但通过用pK为5.8的酸滴定至较低pH值可使其去淬灭。还对两种抗蛋白酶的PDGF突变体（[Ser28]-和[Pro32]-PDGF-BB）进行了表征，结果表明它们的二级和三级结构与野生型PDGF-BB没有区别。因此，这些是适合进行PDGF-BB结构-活性关系研究的稳定背景分子。
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