Significance of the intact polypeptide chains of human fibrinogen in ADP-induced platelet aggregation
Significance of the intact polypeptide chains of human fibrinogen in ADP-induced platelet aggregation
复制标题
人纤维蛋白原完整多肽链在 ADP 诱导血小板聚集中的意义
DOI:
10.1182/blood.v49.4.635.bloodjournal494635
复制
发表时间:
1977
期刊:
影响因子:
20.3
通讯作者:
B. Lipinski
中科院分区:
文献类型:
--
作者:
S. Niewiarowski;A. Budzynski;B. Lipinski
The presence of human fibrinogen in suspensions of washed human platelets is a requirement for ADP-induced platelet aggregation. Digestion of fibrinogen with plasmin destroys this function of the protein. The high solubility fraction of Kabi fibrinogen, fragment X (stage 1) and framgent X (stage 2), are two, eight, and ten times, respectively, less potent in promoting ADP-induced platelet aggregation, as compared with intact fibrinogen. Fragments Y and D and the mixture of reduced and carboxymethylated chains of human fibrinogen do not support ADP-induced platelet aggregation at all. SDS polyacrylamide gel electrophoresis of nonreduced and reduced fibrinogen and its derivatives indicates that the intact fibrinogen molecule is essential for ADP-induced platelet aggregation. It is suggested that the carboxy-terminal part of the Aalpha chain and possibly also the amino-terminal part of the Bbeta chain are required for the platelet aggregation-promoting function of fibrinogen.