油桐尺蠖核型多角体病毒多角体蛋白的理化性质及二级结构预测

由SDS及梯度胶电泳测得油桐尺蠖核型多角体病毒（BsNPV）多角体蛋白天然状态及亚基分子量分别为363kD与31.5kD，从而推断此蛋白为十二聚体，亚基间无二硫键作用．BsNPV多角体蛋白的远紫外圆二色谱显示，它的二级结构含有31．7％的α螺旋，23．8％的β折叠及44．5％的无规卷曲，与二级结构预测结果相符．通过荧光光谱实验推知，BsNPV多角体蛋白的表面疏水性弱，其色氨酸残基位于蛋白疏水核内部．

Physicochemical Properties and Secondary Structure Prediction of Buzura suppressaria Nuclear Polyhedrosis Virus Polyhedrin

Using SDS-PAGE and gel concentration gradient electrophoresis,It was determined that the molecular weights of Buzura suppressaria nuclear polyhedrosis virus (BsNPV) polyhedrin and its subunit are 363 kD and 31. 5 kD respectively and this protein was composed of twelve subunits without disulfide bonds among the subunits. The circular dichroism (CD) spectrum indicated that the secondary structure of polyhedrin consisted of 31, 7 % α-helix, 23. 8% βsheet,and 44. 5 % random-coil,which was in coincidence with the result of prediction. The fluoresence studies of polyhedrin showed that the surface hydrophobicity of polyhedrin was weak and the tryptophan residues in each subunit were in the internal hydrophobic region.