Interaction between Semi-alkaline Proteinase and Protease Inhibitors of Rabbit Serum(Biological)

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Interactions in vitro and in vivo between semi-alkaline proteinase (SAP) and protcase inhibitors of rabbit serum were studied. Avs a result of the purification of SAP inhibitors from rabbit serum, the caseinolytic activity of SAP was found to be inhibited by α_1-macroglobulin (α_1M) and α_1-proteinase inhibitor (α_1PI). SAP was stoichiometrically bound to α_1M at a molar ratio of 1:1 and the proteolytic activity remained constant at 16% of the original activity even in the presence of excess α_1M. In contrast, the proteolytic activity of SAP decreased linearly with increase in the amount of α_1PI, but a 10-fold molar excess of α_1PI was needed for complete inhibition. The disappearance rate of intravenously injected ^<125>I-labeled SAP (^<125>I-SAP) from rabbit serum was also investigated by using high-performance liquid chromatography (HPLC), Serum levels of ^<125>I-SAP decreased biexponentially after a single injection. The results of gel-permeation HPLC of rabbit serum on a TSK G-3000 SW column indicated that SAP was mainly bound to α-macroglobulins and that α-macroglobulin-SAP complex was cleared from the blood circulation with a half-life of 10 min.
社団法人日本薬学会の論文
1987-03-25