Heller K B
J Bacteriol. 1978 Jun;134(3):1181-3. doi: 10.1128/jb.134.3.1181-1183.1978.
The apparent molecular weights of the two forms of a heat-modifiable protein from the outer membrane of Escherichia coli K-12, estimated in gels with different concentrations of acrylamide, indicate that the protein binds excess amounts of sodium dodecyl sulfate, possibly due to large beta structures before boiling.
在含有不同浓度丙烯酰胺的凝胶中对来自大肠杆菌K-12外膜的一种热可修饰蛋白的两种形式的表观分子量进行估计,结果表明该蛋白结合了过量的十二烷基硫酸钠,这可能是由于煮沸前存在较大的β结构。