Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein

T. L. Wasmoen, M. P. Bell, D. A. Loegering, G. J. Gleich, F. G. Prendergast, D. J. McKean

Research output: Contribution to journalArticle

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Abstract

Eosinophil granule major basic protein (MBP) is a relatively low molecular weight cationic (pI > 10) protein present in the crystalloid core of the eosinophil granule. Amino acid sequence analysis of this protein was undertaken as part of an analysis of the structural basis of the potent cytotoxic activities of MBP on parasites and mammalian cells. Many conventional sequencing strategies were unworkable because of the unusual amino acid composition of MBP and its insolubility in solutions buffered at neutral pH. Less conventional chemical reactions, including cyanogen bromide-induced cleavage at tryptophan and acid-induced cleavage at aspartic acid, were used successfully to obtain peptides which allowed definition of the amino acid sequence of MBP. Characterization of MBP by reverse-phase high pressure liquid chromatography and two-dimensional gel analysis showed no microheterogeneity that might be attributed to post-translational modifications. Comparison of the MBP sequence with a protein sequence data base showed that MBP has no significant sequence homology with other characterized proteins. The basicity (pI 10.9) and hydrophobicity predicted from the MBP sequence are likely responsible for the observed affinity of this cytotoxic molecule for cell surfaces and some serum proteins.

Original languageEnglish (US)
Pages (from-to)12559-12563
Number of pages5
JournalJournal of Biological Chemistry
Volume263
Issue number25
StatePublished - 1988

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Protein Sequence Analysis
Amino Acids
Proteins
human PRG2 protein
Eosinophil Major Basic Protein
High pressure liquid chromatography
Cyanogen Bromide
Reverse-Phase Chromatography
Post Translational Protein Processing
Sequence Homology
Hydrophobic and Hydrophilic Interactions
Eosinophils
Aspartic Acid
Tryptophan
Hydrophobicity
Alkalinity
Blood Proteins
Amino Acid Sequence
Parasites
Chemical reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Wasmoen, T. L., Bell, M. P., Loegering, D. A., Gleich, G. J., Prendergast, F. G., & McKean, D. J. (1988). Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. Journal of Biological Chemistry, 263(25), 12559-12563.

Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. / Wasmoen, T. L.; Bell, M. P.; Loegering, D. A.; Gleich, G. J.; Prendergast, F. G.; McKean, D. J.

In: Journal of Biological Chemistry, Vol. 263, No. 25, 1988, p. 12559-12563.

Research output: Contribution to journalArticle

Wasmoen, TL, Bell, MP, Loegering, DA, Gleich, GJ, Prendergast, FG & McKean, DJ 1988, 'Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein', Journal of Biological Chemistry, vol. 263, no. 25, pp. 12559-12563.
Wasmoen TL, Bell MP, Loegering DA, Gleich GJ, Prendergast FG, McKean DJ. Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. Journal of Biological Chemistry. 1988;263(25):12559-12563.
Wasmoen, T. L. ; Bell, M. P. ; Loegering, D. A. ; Gleich, G. J. ; Prendergast, F. G. ; McKean, D. J. / Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 25. pp. 12559-12563.
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