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Purification of two species of exudate cysteine‐proteinase inhibitors that are acute‐phase reactants in the carrageenin‐induced inflammation in rats
Author(s) -
Nakagawa Hideo,
Hirata Kazunari
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80012-6
Subject(s) - exudate , papain , chemistry , isoelectric point , cysteine , affinity chromatography , chromatography , biochemistry , acute phase protein , polyacrylamide gel electrophoresis , sepharose , inflammation , enzyme , biology , immunology , botany
Two species of cysteine‐proteinase inhibitors (CPIs) have been purified to homogeneity from exudate in the carrageenin‐induced inflammation in rats. The exudate CPIs were separated into two forms (named CPI‐1 and ‐2) in affinity chromatography on S ‐carboxymethyl‐papain‐Sepharose, the final stage of purification. CPI‐1 and ‐2 gave different mobilities in polyacrylamide gel electrophoresis (PAGE), probably because of different isoelectric points (p I 4.47 for CPI‐1 and p I 4.21 for CPI‐2). Both CPI‐1 and ‐2 showed immunological identity in double immunodiffusion and same molecular mass of 68 kDa when analysed by SDS‐PAGE. These results indicate that CPI‐1 and ‐2 are very similar but distinct CPIs. CPI‐1 and ‐2 are acute‐phase reactants and probably represent two species of T‐kininogens having inhibitory activity toward cysteine proteinases.