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机构地区:[1]四川大学生物系
出 处:《生物化学杂志》1995年第4期446-451,共6页
基 金:国家自然科学基金
摘 要:以A.niger来源的果胶酶为材料,经过CM-SephadexC-50及SephadexG-100两步骤分离纯化得到电泳均一的endo-PG1及endo-PG2,其亚基分子量分别为35kD及37kD,含糖量为11.22%及8.3%,最大紫外吸收峰分别在274nm及269nm处,氨基酸组成分析结果表明Gly含量较高,Met含量较低,不含Cys,并且酸性氨基酸含量高于碱性氨基酸,圆二色谱结果表明二级结构主要为α螺旋和β折叠,其中endo-PG1含α螺旋45.1%,β折叠24.9%;endo-PG2含α螺旋39.6%,β折叠36.5%。Endo-polygalacturonase (endo-PG1 and endo-PG2) was purified from a commercial preparation of Aspergillus niger pectinase by means of CM-Sephadex C-50 and Sephadex G-100 chromatography. These enzymes were electrophoretically homogeneous and the molecular weights of the subunits were 35kD (endo-PG1)and 37kD (endo-PG2). The two endo-PG displayed UV spectra with a maximam at 274nm and 269nm. Analysis showed that endo-PG had the following total sugar contents (W/W) : 11.22% (endo-PG1) and 8. 3% (endo-PG2) . The amino acid compositions of the two endo-PG were very similar:the Gly content was the highest and Met was lower,there was no Cys,acidic amino acid content was higher than basic amino acid. The CD spectra showed that endo-PG1 contained about 45. 1% α-helix,24. 9% β-pleated sheet, and endo-PG2 contained about 39. 6% α-helix, 36. 5% β-pleated sheet.
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