Degradation of Bovine P2 Protein by Bovine Brain Cathepsin D

Overview

Journal Neurochem Res

Specialties Chemistry
Neurology

Date 1984 Oct 1

PMID 6083469

Citations 2

Authors

J N Whitaker

J M Seyer

Affiliations

Soon will be listed here.

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.

Citing Articles

Proteinases in inflammatory demyelinating disease.

Bever C, Whitaker J Springer Semin Immunopathol. 1985; 8(3):235-50.

PMID: 3901368 DOI: 10.1007/BF00197298.

Susceptibility of myelin proteins to a neutral endoproteinase: the degradation of myelin basic protein (MBP) and P2 protein by purified bovine brain multicatalytic proteinase complex (MPC).

Lucas J, Lobo D, Terry E, Hogan E, Banik N Neurochem Res. 1992; 17(12):1261-6.

PMID: 1281293 DOI: 10.1007/BF00968410.

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