title: [Reactions between protease inhibitors in blood plasma and collagen].
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.
authors.forename: N A
authors.initials: NA
authors.lastname: Zorin
authors.forename: S G
authors.initials: SG
authors.lastname: Zhabin
authors.forename: I G
authors.initials: IG
authors.lastname: Kozlov
authors.forename: N K
authors.initials: NK
authors.lastname: Gorlina
authors.forename: T O
authors.initials: TO
authors.lastname: Iarovinskiĭ
authors.forename: A Iu
authors.initials: AIu
authors.lastname: Emel'ianov
authors.forename: N N
authors.initials: NN
authors.lastname: Semen'kov
mesh_terms: D000818:Animals; D003094:Collagen / Q000097:blood*; D051379:Mice; D011480:Protease Inhibitors / Q000097:blood*; D013379:Substrate Specificity
chemical_list: D011480:Protease Inhibitors; D003094:Collagen