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Using purification procedures, which included acetone precipitation in the presence of CaCl2, Lysine-aminohexyl-Sepharose chromatography and DEAE-Sepharose chromatography, four forms of kallikrein were obtained from hog pancreas autolysate. Lysine-aminohexyl-Sepharose chromatography was particularly effective for obtaining a partially purified preparation, which was then readily fractionated into four homogeneous forms. The total yield of the four forms of kallikrein was about 220 mg from 10 kg of fresh hog pancreas, which was several times higher than those reported by Zuber and Sache (5) and Kira et al. (6). By DEAE-Sephadex A-50 chromatography the partially purified preparation gave two forms, which apparently corresponded to kallikreins A and B reported by Fiedler et al. (2), Kira et al. (6), and Ikekita et al. (23). Further purification was carried out by Zuber and Sache (3) and Kira et al. (6), who reported the occurrence of a third form of kallikrein. Very recently Fiedler and Hirschauer (7) reported the isolation of a fourth form. However, these additional forms were regarded as minor fractions due to insufficient purification. We applied DEAE-Sepharose CL-6B chromatography directly to the partially purified preparation instead of purifying kallikreins A and B separately. Four forms of kallikrein were obtained reproducibly, with yields of 1 : 0.9 : 0.9 :0.6 on a weight basis for kallikreins I—IV, respectively. Polyacrylamide gel electrophoresis revealed that kallikrein A corresponded to kallikreins III plus IV and kallikrein B I plus II. It is unlikely that these four forms are produced by non-specific cleavage of prokallikrein occurring during the autolysis, since the N-terminal sequences are consistent with those reported by Tschesche et al.(22) for kallikreins A and B. |
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