<原著>マウス血漿ムリノグロブリンとα-マクログロブリン : プロテイナーゼ阻害スペクトルと代謝

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This study examined the inhibitory spectrum and catabolism of mouse α-macroglobulin (αM) and mouse murinoglobulin (MU). When injected into lateral tail vein of ICR mouse both ^<125>I-αM complexed with trypsin and ^<125>I-MU complexed with chymotrypsin were rapidly cleared from circulation with half-times of about 5 min. In contrast the half-times for native inhibitors were more than 60 min. When ^<125>I-MU-chymotrypsin complex was injected simultaneously with 50-fold molar excess of unlabeled αM-trypsin complex, the half-time of the labeled protein increased to about 30 min. No rapid clearance was observed, however, for ^<125>I-MU-trypsin complex. The half-lives of desialylated ^<125>I-MU and ^<125>I-αM were about 5 min and 20 min, respectively, but they were prolonged by simultaneous injection of unlabeled asialo-orosomucoid. Heat-denatured ^<125>I-MU and ^<125>I-αM were removed from blood with halftimes of about 3 min, which were prolonged by simultaneous administration of 200-fold molar excess of formaldehyde-treated albumin. These results indicate 1) that MU has a proteinase-binding spectrum similar to that of αM, but is weaker in the ability to protect the bound proteinases from inactivation by the proteinaceous inhibitors than αM, 2) that mouse αM has essentially the same inhibitory spectrum as the human homologue, and 3) that mouse αM and MU are cleared from circulation via three different specific receptors, i. e. for conformationally changed αM, desialylated glycoproteins, and denatured proteins.
近畿大学の論文
1990-06-25

<原著>マウス血漿ムリノグロブリンとα-マクログロブリン : プロテイナーゼ阻害スペクトルと代謝

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