Giasuddin A S, Lehner T, Evans R W
Immunology. 1983 Dec;50(4):651-8.
A small molecular weight streptococcal antigen of about 3800 was isolated from Streptococcus mutans. The peptide was obtained by gel filtration of a predominantly 185,000 mol. wt. antigen preparation, with two major antigenic determinants (I/II), on Sephacryl S-200, in the presence of sodium dodecyl sulphate (SDS). The 185,000 mol. wt. antigen was prepared from the culture supernatant of S. mutans by ammonium sulphate precipitation, DEAE cellulose chromatography and gel filtration on Sepharose 6B. The 3800 mol. wt. material gave a single band on SDS/polyacrylamide gel and reacted with antisera to streptococcal antigen I/II, I and II but not III. Furthermore, it was digested by pronase, contained only traces of carbohydrate and lipids were not detected. It is suggested that SA I/II is either synthesized in a range of molecular sizes from 185,000 to 3800 or the former is broken down by streptococcal proteases into smaller fragments.
从变形链球菌中分离出一种分子量约为3800的小分子链球菌抗原。该肽是通过在十二烷基硫酸钠（SDS）存在下，对主要为185,000分子量的抗原制剂在Sephacryl S - 200上进行凝胶过滤获得的，该制剂具有两个主要抗原决定簇（I/II）。185,000分子量的抗原是通过硫酸铵沉淀、DEAE纤维素色谱法以及在Sepharose 6B上进行凝胶过滤，从变形链球菌的培养上清液中制备的。分子量为3800的物质在SDS/聚丙烯酰胺凝胶上呈现单一条带，并与抗链球菌抗原I/II、I和II的抗血清发生反应，但不与III反应。此外，它能被链霉蛋白酶消化，仅含有微量碳水化合物，未检测到脂质。有人提出，SA I/II要么以从185,000到3800的一系列分子大小合成，要么前者被链球菌蛋白酶分解成更小的片段。
