Literature DB >> 8137941

Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein.

C Oxvig1, G J Gleich, L Sottrup-Jensen.   

Abstract

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 (Cys2, Cys23, Cys42, Cys64, and Cys96), while 4 form disulfides (Cys20-Cys115, and Cys92-Cys107).

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Year:  1994        PMID: 8137941     DOI: 10.1016/0014-5793(94)80459-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

Review 1.  Eosinophils: multifaceted biological properties and roles in health and disease.

Authors:  Hirohito Kita
Journal:  Immunol Rev       Date:  2011-07       Impact factor: 12.988

Review 2.  Eosinophil granule proteins: form and function.

Authors:  K Ravi Acharya; Steven J Ackerman
Journal:  J Biol Chem       Date:  2014-05-06       Impact factor: 5.157

3.  Human alpha2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3.

Authors:  Ninh Doan; Peter G W Gettins
Journal:  Biochem J       Date:  2007-10-01       Impact factor: 3.857

4.  Human eosinophil major basic protein 2: location of disulfide bonds and free sulfhydryl groups.

Authors:  Lori A Wagner; Lyo E Ohnuki; Krishna Parsawar; Gerald J Gleich; Chad C Nelson
Journal:  Protein J       Date:  2007-01       Impact factor: 4.000

  4 in total

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