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Intracellular Protein Catabolism II pp 317–326Cite as

Isolation and Some Properties of Horse Leucocyte Neutral Proteases

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Summary

Horse blood leucocyte granules were found to contain three elastase-like neutral proteases (m.w. 38.000, 24.000 and 20.500, pi 5.3, 8.8 and above 10, respectively). The latter two enzymes were purified to apparent homogeneity by subcellular fractionation, Sephadex G-75 filtration and column chromatography on CM-Sephadex. Their specificity was examined using natural and synthetic substrates. Structure of the active centre was investigated using DFP, isocyanates, photoinactivation with Rose Bengal and iodination with ICI.

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Author information

Authors and Affiliations

  1. Institute of Molecular Biology, Jagiellonian University, Krakow, 31-001, Poland

    Aleksander Koj, Adam Dubin & Jerzy Chudzik

Authors
  1. Aleksander Koj
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  2. Adam Dubin
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  3. Jerzy Chudzik
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Editor information

Editors and Affiliations

  1. Department of Biochemistry J. Stefan Institute, University of Ljubljana, Ljubljana, Yugoslavia

    Vito Turk

  2. New York State Research Institute for Neurochemistry and Drug Addiction, Ward’s Island, New York, USA

    Neville Marks

  3. Strangeways Research Laboratory, Cambridge, C BI 4RN, England

    Alan J. Barrett

  4. Department of Biochemistry and Medicine, University of Miami School of Medicine, Miami, Florida, USA

    J. Frederick Woessner

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© 1977 J. Stefan Institute, Ljubljana, Yugoslavia

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Koj, A., Dubin, A., Chudzik, J. (1977). Isolation and Some Properties of Horse Leucocyte Neutral Proteases. In: Turk, V., Marks, N., Barrett, A.J., Woessner, J.F. (eds) Intracellular Protein Catabolism II. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8813-9_41

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  • DOI: https://doi.org/10.1007/978-1-4615-8813-9_41

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-8815-3

  • Online ISBN: 978-1-4615-8813-9

  • eBook Packages: Springer Book Archive

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