Myllylä R, Anttinen H, Risteli L, Kivirikko K I
Biochim Biophys Acta. 1977 Jan 11;480(1):113-21. doi: 10.1016/0005-2744(77)90326-6.
Collagen glucosyltransferase was isolated as a homogeneous protein from chick embryos by a procedure consisting of ammonium sulphate fractionation, two affinity chromatographies and two gel filtrations. The specific activity of the purified enzyme was 32,000 times that of the 15,000 x g supernatant of the embryo homogenate, and the enzyme was pure when examined by sodium dodecyl sulphate polyacrylamide gel electrophoresis using three different gel compositions. The molecular weight of the enzyme was about 72,000-78,000 by sodium dodecyl sulphate polyacrylamide gel electrophoresis, the value being dependent on the gel composition. The apparent molecular weight by gel filtration was dependent on the purity and protein concentration. The sedimentation coefficient S20,w was 4.7. The data suggest that the enzyme molecule consists of one polypeptide chain.
通过由硫酸铵分级分离、两次亲和层析和两次凝胶过滤组成的程序，从鸡胚中分离出胶原葡萄糖基转移酶，该酶为均一蛋白质。纯化酶的比活性是胚胎匀浆15,000×g上清液的32,000倍，当使用三种不同凝胶组成的十二烷基硫酸钠聚丙烯酰胺凝胶电泳进行检测时，该酶是纯的。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳测定，该酶的分子量约为72,000 - 78,000，该值取决于凝胶组成。通过凝胶过滤测定的表观分子量取决于纯度和蛋白质浓度。沉降系数S20,w为4.7。数据表明该酶分子由一条多肽链组成。
