Panicker M M, Minkley E G
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
J Biol Chem. 1992 Jun 25;267(18):12761-6.
Using a traD overexpression plasmid, we purified the F sex factor TraD protein in milligram quantities. The purified protein has an apparent molecular weight of 82,000 and an amino acid composition rich in acidic residues. Using specific antibodies, TraD was localized to the inner membrane of F+ cells under conditions where it is produced in physiologically normal amounts. Furthermore, the protein was soluble only in the presence of detergents, but there is evidence that the carboxyl terminus is water-soluble. The purified protein shows pH-sensitive binding to DNA cellulose columns.
使用traD过表达质粒，我们以毫克量纯化了F性因子TraD蛋白。纯化后的蛋白表观分子量为82,000，氨基酸组成富含酸性残基。使用特异性抗体，在TraD以生理正常量产生的条件下，它定位于F +细胞的内膜。此外，该蛋白仅在存在去污剂的情况下可溶，但有证据表明其羧基末端是水溶性的。纯化后的蛋白对DNA纤维素柱表现出pH敏感的结合。
