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十二烷基硫酸钠与各种蛋白质的结合。

The binding of sodium dodecyl sulphate to various proteins.

作者信息

Pitt-Rivers R, Impiombato F S

出版信息

Biochem J. 1968 Oct;109(5):825-30. doi: 10.1042/bj1090825.

Abstract
  1. The binding of sodium dodecyl sulphate to proteins by equilibrium dialysis was investigated. 2. Most of the proteins studied bound 90-100% of their weight of sodium dodecyl sulphate. 3. The glycoproteins studied bound 70-100% of their weight of sodium dodecyl sulphate, calculated in terms of the polypeptide moiety of the molecule. 4. Proteins not containing S.S groups bound about 140% of their weight of sodium dodecyl sulphate. 5. Reduction of four proteins containing S.S groups caused a rise in sodium dodecyl sulphate binding to 140% of the weight of protein. 6. The apparent micellar molecular weights of the protein-sodium dodecyl sulphate complexes were measured by the dye-solubilization method; they were all found to have approximately the same micellar molecular weight (34000-41000) irrespective of the molecular weight of the protein to which they were attached.
摘要
  1. 通过平衡透析研究了十二烷基硫酸钠与蛋白质的结合情况。2. 大多数所研究的蛋白质结合了其重量90 - 100%的十二烷基硫酸钠。3. 所研究的糖蛋白结合了其重量70 - 100%的十二烷基硫酸钠,以分子的多肽部分计算。4. 不含二硫键的蛋白质结合了约其重量140%的十二烷基硫酸钠。5. 对四种含二硫键的蛋白质进行还原导致十二烷基硫酸钠结合量增加至蛋白质重量的140%。6. 采用染料增溶法测定了蛋白质 - 十二烷基硫酸钠复合物的表观胶束分子量;发现它们无论与何种分子量的蛋白质结合,都具有大致相同的胶束分子量(34000 - 41000)。

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