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 language | English (US) |
|---|---|
| Pages (from-to) | 12559-12563 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 263 |
| Issue number | 25 |
| State | Published - 1988 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
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 journal › Article
}
TY - JOUR
T1 - Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein
AU - Wasmoen, T. L.
AU - Bell, M. P.
AU - Loegering, D. A.
AU - Gleich, G. J.
AU - Prendergast, F. G.
AU - McKean, D. J.
PY - 1988
Y1 - 1988
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0024210543&partnerID=8YFLogxK
M3 - Article
C2 - 3410852
AN - SCOPUS:0024210543
VL - 263
SP - 12559
EP - 12563
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 25
ER -