Di Scipio R G, Hermodson M A, Yates S G, Davie E W
Biochemistry. 1977 Feb 22;16(4):698-706. doi: 10.1021/bi00623a022.
Human prothrombin, factor IX, and factor X have been idolated in high yield and characterized as the their amino-terminal sequence, molecular weight, amino acid composition, and migration in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. An additional human plasma protein, called protein S, has also been purified and its properties have been compared with those of prothrombin, factor IX, and factor X. Prothrombin (mol wt 72 000), factor IX (mol wt 57 000), and protein S (mol wt 69 000) are single-chain glycoproteins, while factor X (mol wt 59 000) is a glycoprotein composed of two polypeptide chains held together by a disulfide bond(s). The amino-terminal sequence of the light chain of human factor X is homologous with prothrombin, factor IX, and protein S. The heavy chain of human factor X is slightly larger than the heavy chain of bovine factor X and differs from bovine factor X in its amino-terminal sequence.
人凝血酶原、因子IX和因子X已被高产率分离出来，并对其氨基末端序列、分子量、氨基酸组成以及在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳中的迁移情况进行了表征。另一种人血浆蛋白，称为蛋白S，也已被纯化，并将其性质与凝血酶原、因子IX和因子X的性质进行了比较。凝血酶原（分子量72000）、因子IX（分子量57000）和蛋白S（分子量69000）是单链糖蛋白，而因子X（分子量59000）是由通过二硫键连接在一起的两条多肽链组成的糖蛋白。人因子X轻链的氨基末端序列与凝血酶原、因子IX和蛋白S同源。人因子X的重链比牛因子X的重链略大，并且在氨基末端序列上与牛因子X不同。
