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人体血液中去精氨酸纤维蛋白肽B的测定

Measurement of desarginine fibrinopeptide B in human blood.

作者信息

Eckhardt T, Nossel H L, Hurlet-Jensen A, La Gamma K S, Owen J, Auerbach M

出版信息

J Clin Invest. 1981 Mar;67(3):809-16. doi: 10.1172/JCI110098.

Abstract

Thrombin converts fibrinogen to fibrin in two steps. First fibrinopeptide A and fibrin I are formed and then fibrinopeptide B (B beta 1-14) and fibrin II. Since it is postulated that fibrin II is important in the genesis of thrombosis, it is of interest to measure fibrinopeptide B in peripheral blood samples. Previous difficulties in interpreting fibrinopeptide B immunoreactivity in plasma resulted from crossreaction of fibrinogen and of plasmin digest peptides B beta 1-42 and B beta 1-21 and from rapid loss of fibrinopeptide B immunoreactivity resulting from cleavage of arginine 14 by blood carboxypeptidase B. We have obviated these difficulties by removing fibrinogen from plasma by precipitation with ethanol and peptides B beta 1-21 and B beta 1-42 by adsorption on bentonite. Fibrinopeptide B is then converted to a desarginine fibrinopeptide B, which is measured in a new specific assay. Studies of the kinetics of fibrinopeptide cleavage showed that when whole blood was allowed to clot in vitro, fibrinopeptide A was cleaved more rapidly than fibrinopeptide B. In 18 patients on an acute care medical ward, desarginine fibrinopeptide B levels were lower than fibrinopeptide A levels and did not correlate with the levels of fibrinopeptide A or B beta 1-42. Desarginine fibrinopeptide B levels were less than 1 pmol/ml in all but two patients. In six patients receiving intraamniotic infusions of hypertonic saline to induce abortion, desarginine fibrinopeptide B levels increased 10-fold from the preinfusion mean level of 0.4 pmol/ml and then decreased. The pattern of changes resembled that of the fibrinopeptide A levels rather than of the B beta 1-42 levels. On the basis of these data it is suggested that plasma desarginine fibrinopeptide B levels reflect fibrin II formation in vivo.

摘要

凝血酶分两步将纤维蛋白原转化为纤维蛋白。首先形成纤维蛋白肽A和纤维蛋白I,然后形成纤维蛋白肽B(Bβ1 - 14)和纤维蛋白II。由于推测纤维蛋白II在血栓形成过程中很重要,因此测量外周血样本中的纤维蛋白肽B很有意义。以往在解释血浆中纤维蛋白肽B免疫反应性时遇到困难,原因是纤维蛋白原以及纤溶酶消化肽Bβ1 - 42和Bβ1 - 21的交叉反应,还有血液羧肽酶B对精氨酸14的切割导致纤维蛋白肽B免疫反应性迅速丧失。我们通过用乙醇沉淀从血浆中去除纤维蛋白原,并通过膨润土吸附去除肽Bβ1 - 21和Bβ1 - 42,避免了这些困难。然后将纤维蛋白肽B转化为去精氨酸纤维蛋白肽B,通过一种新的特异性检测方法进行测量。纤维蛋白肽切割动力学研究表明,当全血在体外凝固时,纤维蛋白肽A的切割速度比纤维蛋白肽B快。在急性护理病房的18名患者中,去精氨酸纤维蛋白肽B水平低于纤维蛋白肽A水平,且与纤维蛋白肽A或Bβ1 - 42水平无关。除两名患者外,所有患者的去精氨酸纤维蛋白肽B水平均低于1 pmol/ml。在六名接受羊膜腔内输注高渗盐水引产的患者中,去精氨酸纤维蛋白肽B水平从输注前的平均水平0.4 pmol/ml增加了10倍,然后下降。变化模式类似于纤维蛋白肽A水平,而不是Bβ1 - 42水平。基于这些数据,提示血浆去精氨酸纤维蛋白肽B水平反映体内纤维蛋白II的形成。

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1
Human fibrinopeptides. Isolation, characterization and structure.人纤维蛋白肽。分离、特性及结构。
Biochim Biophys Acta. 1966 Feb 28;115(2):371-96. doi: 10.1016/0304-4165(66)90437-5.
2
3
Measurement of fibrinopeptide A in human blood.人体血液中纤维蛋白肽A的测定。
J Clin Invest. 1974 Jul;54(1):43-53. doi: 10.1172/JCI107749.

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