α与蛋白酶2-macroglobulin之间的交互。特征和特异性的反应,其分子机制和假设。

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巴雷特AJ,斯达克点

α与蛋白酶2-macroglobulin之间的交互。特征和特异性的反应,其分子机制和假设。

j . 1973年8月,133 (4):709 - 24。doi: 10.1042 / bj1330709。

PubMed ID

4201304 (在PubMed

]

文摘

1。α(2)巨球蛋白是绑定和抑制丝氨酸蛋白酶。我们表明,它结合硫醇和羧基蛋白酶,现在有理由相信α(2)巨球蛋白可以绑定基本上所有蛋白酶。2。放射化学标签胰蛋白酶、胰凝乳蛋白酶、组织蛋白酶B1和木瓜蛋白酶是受α(2)巨球蛋白在一个大约克分子数相等的比例。克分子数相等的绑定被确认为胰蛋白酶activesite滴定。3所示。预处理的α(2)巨球蛋白数量饱和的一个蛋白酶阻止随后的绑定的另一个地方。我们得出这样的结论:每个分子α(2)巨球蛋白能够与一个分子反应的蛋白酶。4所示。 alpha(2)-Macroglobulin did not react with exopeptidases, non-proteolytic hydrolases or inactive forms of endopeptidases. 5. The literature on binding and inhibition of proteinases by alpha(2)-macroglobulin is reviewed, and from consideration of this and our own work several general characteristics of the interaction can be discerned. 6. A model is proposed for the molecular mechanism of the interaction of alpha(2)-macroglobulin with proteinases. It is suggested that the enzyme cleaves a peptide bond in a sensitive region of the macroglobulin, and that this results in a conformational change in the alpha(2)-macroglobulin molecule that traps the enzyme irreversibly. Access of substrates to the active site of the enzyme becomes sterically hindered, causing inhibition that is most pronounced with large substrate molecules. 7. The possible physiological importance of the unique binding characteristics of alpha(2)-macroglobulin is discussed.

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药物靶点

药物	目标	类	生物	药理作用	行动
Anacaulase	Alpha-1-antichymotrypsin	蛋白质	人类	未知的	粘结剂	细节
Anacaulase	Alpha-2-macroglobulin	蛋白质	人类	未知的	粘结剂	细节