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抗铜酿酒酵母铜结合蛋白的纯化及性质研究
引用本文:邢小云,李明春,侯文强,邢来君.抗铜酿酒酵母铜结合蛋白的纯化及性质研究[J].南开大学学报,2000,33(3):63-66.
作者姓名:邢小云  李明春  侯文强  邢来君
作者单位:南开大学微生物学系!天津,300071,南开大学微生物学系!天津,300071,南开大学微生物学系!天津,300071,南开大学微生物学系!天津,300071
摘    要:酿酒酵母Cu^2+抗株YND21经含一定浓度的氯化铜培养基诱导培养后,收集菌体,破碎细胞,离心后SephadexG-50和DEAE-cellulose柱层析分离可获得三种铜结合蛋白DE-1,DE-2,DE-3。DE-1脱盐后(G-1)经鉴定具有金属硫蛋白的特性:表观分子量约为18kD;每分子蛋白含20个巯基,结合11个铜原子;氨基酸组成中富含半胱氨酸(18%)、碱性和酸性氨基酸,而酪氨酸和蛋氨酸含

关 键 词:酿酒酵母  硫硫蛋白  铜诱导  结合蛋白  纯化
修稿时间:1998-12-03

PURIFICATION AND CHARACTERIZATION OF COPPER-BINDING PROTEIN IN A COPPER-RESISTANT STRAIN OF SACCHAROMYCES CEREVISIAE
Xing Xiaoyun,Li Mingchun,Hou Wenqiang,Xing Laijun.PURIFICATION AND CHARACTERIZATION OF COPPER-BINDING PROTEIN IN A COPPER-RESISTANT STRAIN OF SACCHAROMYCES CEREVISIAE[J].Acta Scientiarum Naturalium University Nankaiensis,2000,33(3):63-66.
Authors:Xing Xiaoyun  Li Mingchun  Hou Wenqiang  Xing Laijun
Abstract:Three proteins DE 1,DE 2 and DE 3 were produced from the Cu 2 resistant strain YND21 of Saccharomyces cerevisiae induced with CuCl 2 and isolated by means of Sephadex G 50 and DEAE cellulose column chromatography. The purified Cu binding protein G 1 has the characteristics of metallothioneins:(1) low molecular weight (apparent molecular weight 18000D), (2) high Cu and SH content(each molecule contains 20 thiol groups and combines with 11 copper atoms),(3) amino acid composition rich in cysteine(18%), basic and acidic amino acids but almost free from aromatic amino acids (Tyr)and Met, (4) isoelectric point about 5.13. Purified protein G 1 was shown to be homogeneous by analysis of SDS PAGE and IEF, and largely consistent with the metallothioneins reported.
Keywords:Saccharomyces cerevisiae  metal inductivity  metallothionein  purification
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