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Studies on Kininogen from Sheep Plasma

Kininogens are large molecular mass cysteine proteinase inhibitors belonging to class 3 of the cystatin superfamily. They are single-chain proteins composed of an N-terminal heavy chain, the bradykinin moiety and a C-terminal light chain held together by disulphide bridges. On the bases of their differences in size, structure and functions, kininogens of mammalian plasma have been divided into three classes i) high molecular weight kininogen (HMWK-MW 88-114 kDa) ii) low molecular weight kininogen (LMWK-MW of 50-68 kDa) and iii) T kininogen (MW 68 kDa). Important functions of kininogens are the release of vasoactive peptide bradykinin. by acting as a substrate for kallikrein, intrinsic blood coagulation, acute phase reactions and inhibition of cysteine proteinases. Present study describes the isolation, purification and physico-chemical characterization of these inhibitors from sheep plasma. Kininogens have been characterized from many mammals including human, bovine, rat and recently from whale. Kininogens (HMWK, LMWKl and LMWK2) were purified to apparent homogeneity from sheep (Av/s Arias) plasma by simple three step procedure i.e. ammonium sulphate precipitation, column chromatography on Sephacryl-300HR and ion exchange chromatography on DEAE cellulose. Protein precipitated between 40-60% ammonium sulphate saturation was dialyzed and loaded on S-300HR column. Two protein peaks with papain inhibitory activity were obtained. First peak corresponded to HMWK that was found to be homogenous on native PAGE. Second peak, which corresponds to LMWK, was heterogeneous and was further purified by ion exchange chromatography on DEAE cellulose column. Two protein peaks were obtained from ion exchange column corresponding to two isoforms LMWKl and LMWK2. The two isoforms were found to be homogenous on native PAGE. The yield of HMWK, LMWKl and LMWK2 was about 14.41. 5.63 and 10.65 respectively. Native PAGE and SDS-PAGE indicated that the inhibitors were purified to the extent of homogeneity on the basis of molecular weight and charge. HMWK gave a single band on SDS-PAGE with a molecular weight corresponding to 280 kDa. Under reducing conditions HMWK gave a single band with molecular weight corresponding to 140 kDa indicative of its dimeric nature. Purified LMWKl and LMWK2 demonstrated single bands under reducing and nonreducing conditions, with an apparent molecular weight of 68 kDa. Stokes radii