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Kinins pp 123-133 | Cite as

The Primary Structure of Pig Pancreatic Kallikrein B

  • H. Tschesche
  • W. Ehret
  • G. Godec
  • C. Hirschauer
  • C. Kutzbach
  • G. Schmidt-Kastner
  • F. Fiedler
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 70)

Abstract

Our studies on the amino acid sequence of pig pancreatic kallikrein B (EC 3.4.21.8) have been performed with a preparation (1) that had been treated with neuraminidase to remove bound sialic acids. After reductive cleavage of the disulfide bridges and carboxymethylation, two peaks of UV-absorbing material could be separated by gel filtration on Sephadex G-75 in 50% acetic acid. According to gel electrophoresis, both were essentially homogeneous. Evidently, pig pancreatic kallikrein is composed of two chains presumably held together by disulfide bridges, as it had already been inferred from the presence of two amino terminal and two C-terminal amino acid residues (2).

Keywords

Serine Proteinase Disulfide Bridge Cyanogen Bromide Ammonium Carbonate Porcine Trypsin 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • H. Tschesche
    • 1
  • W. Ehret
    • 2
  • G. Godec
    • 1
  • C. Hirschauer
    • 2
  • C. Kutzbach
    • 3
  • G. Schmidt-Kastner
    • 3
  • F. Fiedler
    • 2
  1. 1.Institute of Organic ChemistryTechnical University of MunichGermany
  2. 2.Institute of Clinical Chemistry and Clinical BiochemistryUniversity of MunichGermany
  3. 3.Farbenfabriken Bayer AGElberfeldGermany

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