Kinins IV pp 211-218 | Cite as

Purification and Partial Characterization of Cat Colon and Submandibular Gland Kallikreins

  • Hiroyuki Fujimori
  • Peter R. Levison
  • Melville Schachter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 198A)


Kallikreins from cat colon and submandibular gland have been purified by acetone fractionation of tissue extracts, DEAE-Sephacel ion-exchange chromatography, ρ-aminobenzamidine Sepharose 4B affinity chromatography and gel filtration on Sephadex G-75. They were of similar M.W., approximately 40,000, and each comprised five forms by isoelectricfocusing (pI 4.1–4.8). Both enzymes were potent kininogenases and exhibited similar specificities with synthetic ester and amide substrates. They were susceptible to a range of protease inhibitors. Surprisingly, neither was sensitive to aprotinin yet both were partially inhibited by soya-bean trypsin inhibitor. They were indistinguishable in our immunological tests.

An acidic esterase (pI 2.2-3.5) of M.W. 120, 000 was isolated from cat stomach by the same procedure. While it exhibited weak immunologic similarity to cat submandibular gland kallikrein, it had negligible kininogenase activity and different substrate and inhibitor specificities to the two kallikreins. It is conclude that similar tissue kallikreins are present in the colon and submandibular gland of the cat but are distinct from this cat stomach esterase.


Submandibular Gland Tissue Kallikrein Precipitin Line Striate Duct Acetone Fractionation 
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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Hiroyuki Fujimori
    • 1
  • Peter R. Levison
    • 1
  • Melville Schachter
    • 2
  1. 1.Alberta Heritage Foundation for Medical Research FellowsEdmontonCanada
  2. 2.Department of PhysiologyUniversity of AlbertaEdmontonCanada

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