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Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein
Author(s) -
Oxvig Claus,
Gleich Gerald J.,
Sottrup-Jensen Lars
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80459-1
Subject(s) - cystine , cysteine , chemistry , disulfide bond , eosinophil , eosinophil granule proteins , biochemistry , major basic protein , residue (chemistry) , granule (geology) , amino acid , stereochemistry , enzyme , biology , immunology , paleontology , asthma
Eosinophil granule major basic protein (117 residues) is known to contain free sulfhydryl groups. Here we have located in the amino acid sequence the half‐cystine residues present as cysteine, and identified those engaged in disulfide bridges. Of the 9 half‐cystine residues, 5 are unpaired cysteines (Cys 2 , Cys 23 , Cys 42 , Cys 64 , and Cys 96 ), while 4 form disulfides (Cys 20 ‐Cys 115 , and Cys 92 ‐Cys 107 ).

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