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On the Specificity of Cathepsin B2

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Intracellular Protein Catabolism II

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Abstract

Cathepsin B2 that evolved eight years ago together with cathepsin B1 (1) from the then cathepsin B — described in 1957 by Greenbaum and Fruton (2) — has, in the meantime, been purified to homogeneity (3). In,gel electrophoresis, it displays two bands, close together and of similar appearance, both of them hydrolyzing benzoylarginineamide (Bz—Arg—NH2). This substrate was the classic substrate for the former cathepsin B and still is a substrate for both cathepsin B1 and B2.

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References

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Author information

Authors and Affiliations

  1. Department of Physiological Chemistry, Division of Enzymology, University of Bonn, Bonn, GFR

    K. Otto, Husan Afroz, R. Müller & P. Fuhge

Authors
  1. K. Otto
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  2. Husan Afroz
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  3. R. Müller
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  4. P. Fuhge
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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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Otto, K., Afroz, H., Müller, R., Fuhge, P. (1977). On the Specificity of Cathepsin B2. 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_36

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  • DOI: https://doi.org/10.1007/978-1-4615-8813-9_36

  • 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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