Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine.
Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine.
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纤维蛋白原京都 II，一种新的先天性异常分子，其特征是 A α 脯氨酸 18 被亮氨酸取代。
DOI：
10.1182/blood.v78.1.149.bloodjournal781149
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发表时间：
1991
期刊：
影响因子：
20.3
通讯作者：
S. Asakura
中科院分区：
文献类型：
--
作者：
N. Yoshida;M. Okuma;H. Hirata;M. Matsuda;K. Yamazumi;S. Asakura
一名患有出血问题的 27 岁女性发现了一例杂合性纤维蛋白原原血症新病例，其特征是纤维蛋白 α 链 NH2 末端区域发生氨基酸替换。她的一期凝血酶原时间和活化部分凝血活酶时间略有延长，该患者纯化的纤维蛋白原的凝血酶或立止血酶时间明显延长。纤维蛋白肽A和B的释放正常，但纤维蛋白单体的聚合受损。还原条件下纯化的纤维蛋白原十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示其三链表观分子量无异常。经赖氨酰内肽酶裂解的纯化 A α 链的反相高效液相色谱 (HPLC) 显示，与正常量相比，一种肽减少，并且出现异常肽峰。这些肽用凝血酶处理并在 HPLC 上进一步分离。异常肽的氨基酸序列分析表明，纤维蛋白α链NH2末端的第二个残基Aα脯氨酸18被亮氨酸取代。合成肽 Gly-Pro-Arg-Pro 抑制凝血酶和爬行动物酶诱导的纤维蛋白聚集，但 Gly-Leu-Arg-Pro 在相同条件下几乎没有或没有显示出抑制作用。这种异常纤维蛋白原的发现支持了以下发现：A α 脯氨酸 18 作为纤维蛋白 α 链 NH2 末端聚合位点的一部分很重要。产妇的母亲也有同样的异常纤维蛋白原。这种独特的遗传性异常纤维蛋白原被命名为纤维蛋白原京都II。
A new case of heterozygous dysfibrinogenemia characterized by an amino acid replacement in the NH2-terminal region of the fibrin alpha-chain was found in a 27-year-old woman with a bleeding problem. Her one-stage prothrombin time and activated partial thromboplastin time were slightly prolonged, and the purified fibrinogen from this patient had a markedly prolonged thrombin or reptilase time. Release of fibrinopeptides A and B was normal, but the polymerization of fibrin monomers was impaired. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified fibrinogen under the reduced condition showed no abnormalities in the apparent molecular weights of its three chains. Reverse-phase high performance liquid chromatography (HPLC) of the lysylendopeptidase-cleaved purified A alpha-chains showed a decrease in one peptide compared with the normal amount and the appearance of an abnormal peptide peak. These peptides were treated with thrombin and further separated on HPLC. Amino acid sequence analysis of the abnormal peptide indicated that A alpha proline-18, the second residue from the NH2-terminus of the fibrin alpha-chain, was replaced by leucine. The synthetic peptide Gly-Pro-Arg-Pro inhibited both thrombin- and reptilase-induced fibrin aggregation, but Gly-Leu-Arg-Pro showed little or no inhibition under the same conditions. The discovery of this abnormal fibrinogen supports the findings that A alpha proline-18 is important as part of the polymerization site in the NH2-terminus of the fibrin alpha-chain. The propositus' mother had the same abnormal fibrinogen. This unique inherited abnormal fibrinogen was designated as fibrinogen Kyoto II.
编码人纤维蛋白原γ链的互补脱氧核糖核酸的表征。
影响因子：
2.9
作者：
Chung,DW;Chan,WY;Davie,EW
通讯作者：
Davie,EW