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Isolation and Characterization of Four Forms of Kallikrein from Hog Pancreas Autolysate1
Four forms of kallikrein, designated as I-IV, were isolated from hog pancreas autolysate mainly by chromatographies on Lysine-aminohexyl-Sepharose and on DEAE-Sepharose CL-6B, with yields of 65, 56, 59, and 41 mg, respectively, from 10 kg of the tissue. They were homogeneous on polyacrylamide gel electrophoresis, indistinguishable from eath other immunologically and had the same amino acid composition. Kallikreins I, II, and III contained carbohydrate, but kallikrein IV was essentially carbohydrate free. On reduction with mercaptoethanol, each of them produced two polypeptide chains with different molecular weights. The H (heavy) chains from kallikreins I and II were identical, designated as Hj. It was a glycoprotein with apparent molecular weight of 21,000, whereas the H chain from III and IV, designated as H,, had a molecular weight of 17,000 and was regarded as an H! chain devoid of carbohydrate. Likewise, the L (light) chain from kallikreins I and III, designated as LL, was a glycoprotein with an apparent molecular weight of 12,000, whereas L, from II and IV corresponded to L^ devoid of carbohydrate and had a molecular weight of 8,500. Thus, kallikreins I-IV could be expressed as Hil^, HiL,, HJLJ, and H,Li, respectively. They had comparable specific activities and Km values towards synthetic substrates. The isoelectric points of kallikreins I-IV were nearly the same, with values of 4.0-4.1.
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