Reactions between protease inhibitors in blood plasma and collagen |
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Zorin N.A., Zhabin S.G., Kozlov I.G., Gorlina N.K., Iarovinskii T.O., Emel'ianov A.Iu., Semen'kov N.N. | PubMed Id: 8619306 | Year: 1995 vol: 41 issue:6 pages: 53-55 | Abstract: The interaction of three macroglobulins and three serpines, as well as inter-alpha-trypsin inhibitor (ITI) with alpha 1- and alpha 2-chains of collagen I which were immobilized on nitrocellulose. All seven proteinase inhibitors were shown to have a certain affinity for collagen. The binding of alpha 2-macroglobulin and gestation-associated protein A with collagen chains is largely determined by the conformational state of these macrophages. alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B. | Download PDF:  | Reference: Zorin N.A., Zhabin S.G., Kozlov I.G., Gorlina N.K., Iarovinskii T.O., Emel'ianov A.Iu., Semen'kov N.N., Reactions between protease inhibitors in blood plasma and collagen, Voprosy meditsinskoi khimii, 1995, vol: 41(6), 53-55. |
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