Goodman P A, Karn R C
Biochem Genet. 1983 Apr;21(3-4):405-16. doi: 10.1007/BF00499148.
The allelically determined human salivary proteins, Ps 1 and 2, were purified on sodium dodecyl sulfate gels, eluted, and compared by limited proteolysis with Streptomyces griseus protease VI, Bacillus subtilis protease VII, and Staphylococcus aureus protease V8. Prior dansylation of the Ps isoproteins facilitated visualization of the peptides. Digestion patterns indicate considerable homology between the Ps isoproteins and support the conclusion [Azen, A. E., and Denniston, C. (1980). Biochem. Genet. 18:483] that there is an actual molecular weight difference between them. Further, the results suggest that this difference owes to an extension of the Ps 2 chain at one of its ends.
通过十二烷基硫酸钠凝胶对由等位基因决定的人类唾液蛋白Ps 1和Ps 2进行纯化、洗脱，然后用灰色链霉菌蛋白酶VI、枯草芽孢杆菌蛋白酶VII和金黄色葡萄球菌蛋白酶V8进行有限蛋白酶解比较。对Ps同工蛋白进行丹磺酰化处理有助于肽段的可视化。消化模式表明Ps同工蛋白之间具有相当大的同源性，并支持这样的结论[Azen, A. E., and Denniston, C. (1980). Biochem. Genet. 18:483]，即它们之间存在实际的分子量差异。此外，结果表明这种差异是由于Ps 2链在其一端的延伸。
