Board P G, Shaw D C
Br J Haematol. 1983 Jun;54(2):245-54. doi: 10.1111/j.1365-2141.1983.tb02092.x.
Prothrombin was purified from normal blood donors and individuals heterozygous for prothrombin type 3. Comparison of the purified prothrombin preparations by tryptic peptide mapping, amino acid analysis and automated sequencing after thrombin digestion, has indicated that prothrombin type 3 results from the substitution of a lysine residue for glutamic acid at position 157. This substitution can result from a single base change in the structural gene and explains the relatively slow electrophoretic mobility of prothrombin type 3 at alkaline pH. An additional thrombin cleavage site in profragment 1 has been identified at arginine 54 by automated sequence analysis of thrombin digests by prothrombin.
从正常献血者和凝血酶原3型杂合个体中纯化凝血酶原。通过胰蛋白酶肽图谱分析、氨基酸分析以及凝血酶消化后的自动测序对纯化的凝血酶原制剂进行比较，结果表明凝血酶原3型是由第157位的谷氨酸被赖氨酸取代所致。这种取代可能源于结构基因中的单个碱基变化，并解释了凝血酶原3型在碱性pH条件下相对较慢的电泳迁移率。通过对凝血酶消化凝血酶原的自动序列分析，已在1号前片段的精氨酸54处鉴定出一个额外的凝血酶切割位点。
