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纤溶酶原:对其生物化学和功能的简要介绍。

Plasminogen: a brief introduction into its biochemistry and function.

作者信息

Miyashita C, Wenzel E, Heiden M

机构信息

Abt. für Klinische Haemostaseologie und Transfusionsmedizin, Universitätskliniken, Homburg/Saar, FRG.

出版信息

Haemostasis. 1988;18 Suppl 1:7-13. doi: 10.1159/000215824.

DOI:10.1159/000215824
PMID:3280426
Abstract

Human plasminogen is a beta-globulin (2% carbohydrate, molecular weight 90 KD), which in its native form has NH2-terminal glutamic acid (Glu-plasminogen) whose primary structure is known (31, 37, 38). From human plasma plasminogen can easily be isolated by affinity chromatography techniques (10, 25, and Table 1). Plasminogen is synthesized in many organs. The production site of the zymogen may be the liver (21), the eosinophiles (3) or the kidney (15). The plasma-plasminogen level is low in newborns (22) and even lower in the premature infant (2). In healthy adults it is found in plasma or serum in a concentration of 200 mg/l (= 2 microM, 22, 39). The half-life of the native (Glu-) plasminogen is 2.24 +/- 0.29 days (6). Two types of Glu-plasminogen occur in human plasma, which differ in their carbohydrate composition as well as in their content of sialic acid. Genetic variants (see Mayr, 3.1.); of plasminogen have been reported (16) after isoelectric focusing of human plasma in polyacrylamide gels. Three patterns were found, two completely different and the third most likely a mixture of the other two. Characteristical functional properties of plasminogen are related to its molecular structure, e.g. its in vivo specificity for fibrin in contrast to the fairly unspecific in vitro activity of plasmin. Glu-plasminogen is easily converted by limited plasmic digestion to modified forms with NH2-terminal lysine, valine or methionine, which are commonly designated "Lys-plasminogen" displaying a plasma half-life time of 0.8 days.(ABSTRACT TRUNCATED AT 250 WORDS)

摘要

人纤溶酶原是一种β球蛋白(含2%碳水化合物,分子量90千道尔顿),其天然形式具有氨基末端谷氨酸(谷氨酸纤溶酶原),其一级结构已知(参考文献31、37、38)。通过亲和层析技术可轻松从人血浆中分离出纤溶酶原(参考文献10、25及表1)。纤溶酶原在许多器官中合成。该酶原的产生部位可能是肝脏(参考文献21)、嗜酸性粒细胞(参考文献3)或肾脏(参考文献15)。新生儿血浆纤溶酶原水平较低(参考文献22),早产儿更低(参考文献2)。在健康成年人中,血浆或血清中的纤溶酶原浓度为200毫克/升(=2微摩尔,参考文献22、39)。天然(谷氨酸)纤溶酶原的半衰期为2.24±0.29天(参考文献6)。人血浆中存在两种类型的谷氨酸纤溶酶原,它们的碳水化合物组成以及唾液酸含量不同。在聚丙烯酰胺凝胶中对人血浆进行等电聚焦后,已报道了纤溶酶原的遗传变异(见迈尔,3.1.)(参考文献16)。发现了三种模式,两种完全不同,第三种很可能是其他两种的混合物。纤溶酶原的特征性功能特性与其分子结构有关,例如其在体内对纤维蛋白的特异性,这与纤溶酶在体外相当非特异性的活性形成对比。谷氨酸纤溶酶原通过有限的血浆消化很容易转化为具有氨基末端赖氨酸、缬氨酸或蛋氨酸的修饰形式,这些通常被称为“赖氨酸纤溶酶原”,其血浆半衰期为0.8天。(摘要截取自250字)

相似文献

1
Plasminogen: a brief introduction into its biochemistry and function.纤溶酶原:对其生物化学和功能的简要介绍。
Haemostasis. 1988;18 Suppl 1:7-13. doi: 10.1159/000215824.
2
Isolation and characterization of the affinity chromatography forms of human Glu- and Lys-plasminogens and plasmins.
J Biol Chem. 1976 Jun 25;251(12):3693-9.
3
Physiology of plasminogen: with special reference to activation and degradation.纤溶酶原的生理学:特别涉及激活与降解
Haemostasis. 1988;18 Suppl 1:25-35. doi: 10.1159/000215834.
4
[Features of the interaction of Glu- and Lys-forms of plasminogen with native and partially hydrolyzed fibrin].
Biokhimiia. 1992 May;57(5):728-37.
5
Physical and chemical properties of the NH2-terminal glutamic acid and lysine forms of human plasminogen and their derived plasmins with an NH2-terminal lysine heavy (A) chain.人纤溶酶原的氨基末端谷氨酸和赖氨酸形式及其衍生的具有氨基末端赖氨酸重链(A链)的纤溶酶的物理和化学性质。
J Biol Chem. 1975 Jun 10;250(11):4044-7.
6
Abnormal plasminogen Maywood I.异常纤溶酶原 梅伍德I型
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A rapid and simple method for the separation of four molecular forms of human plasminogen.一种快速简便的分离人纤溶酶原四种分子形式的方法。
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8
Investigation of a congenital abnormal plasminogen, Frankfurt I, and its relationship to thrombosis.先天性异常纤溶酶原法兰克福I型的研究及其与血栓形成的关系。
Thromb Haemost. 1986 Jun 30;55(3):396-401.
9
Tissue-type plasminogen activator increases the binding of glu-plasminogen to clots.组织型纤溶酶原激活剂可增加谷氨酸纤溶酶原与血栓的结合。
J Clin Invest. 1984 Dec;74(6):2009-16. doi: 10.1172/JCI111623.
10
Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins.在刺激尿激酶型蛋白合成和/或释放的情况下,尿激酶在正常人类受试者肠道中的转运。
J Clin Invest. 1985 Apr;75(4):1212-22. doi: 10.1172/JCI111818.

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