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Degradation of bovine P2 protein by bovine brain cathepsin D

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Abstract

Bovine brain cathepsin D cleaved bovine P2 protein to produce three major and several minor peptides. The major P2 peptides formed were shown by amino acid analysis and partial sequencing to be peptides 17–54, 20–58 and 65–131 with the latter predominating. In preliminary experiments, P2 peptide 65–131 did not induce experimental allergic neuritis in Lewis rats in equimolar amounts to the neuritogenic P2.

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Authors and Affiliations

  1. Research Service of the Memphis Veterans Medical Center, 1030 Jefferson Avenue, 38104, Memphis, Tennessee

    John N. Whitaker & Jerome M. Seyer

  2. Neurology Service of the Memphis Veterans Medical Center, 1030 Jefferson Avenue, 38104, Memphis, Tennessee

    John N. Whitaker

  3. Department of Neurology of the University of Tennessee, Center for the Health Sciences, 1030 Jefferson Avenue, 38104, Memphis, Tennessee

    John N. Whitaker

  4. Department of Anatomy of the University of Tennessee, Center for the Health Sciences, 1030 Jefferson Avenue, 38104, Memphis, Tennessee

    John N. Whitaker

  5. Department of Biochemistry of the University of Tennessee, Center for the Health Sciences, 1030 Jefferson Avenue, 38104, Memphis, Tennessee

    Jerome M. Seyer

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Special issue dedicated to Dr. Elizabeth Roboz-Einstein.

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Whitaker, J.N., Seyer, J.M. Degradation of bovine P2 protein by bovine brain cathepsin D. Neurochem Res 9, 1431–1443 (1984). https://doi.org/10.1007/BF00964670

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