Mass spectrometric analysis reveals a cysteine bridge between residues 2 and 61 of the auxin-binding protein 1 from Zea mays L
| Autor: | Axel Römer, Klaus Palme, Christian Feckler, Werner Feser, Gerhard Muster |
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| Rok vydání: | 2001 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Glycan Stereochemistry Molecular Sequence Data Biophysics Receptors Cell Surface Mass spectrometry Zea mays Biochemistry Residue (chemistry) Structural Biology Genetics Trypsin Electrospray mass spectrometry Amino Acid Sequence Disulfides Auxin-binding protein 1 Molecular Biology Chromatography High Pressure Liquid Plant Proteins Chromatography Molecular mass Functional analysis biology Chemistry Cell Biology Peptide Fragments Maize Protein Structure Tertiary Cysteine bridge Molecular Weight Covalent bond biology.protein Cysteine |
| Zdroj: | FEBS Letters. 509:446-450 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/s0014-5793(01)03196-9 |
| Popis: | The major auxin-binding protein (ZmERabp1) from maize (Zea mays L.) has been structurally characterized. We determined the position of a disulfide bridge in ZmERabp1 by mass-spectrometric analysis. We show that Cys2 and Cys61 are covalently linked and that residue Cys155 bears the free sulfhydryl group. By making use of electrospray mass spectrometry, the molecular mass of ZmERabp1 was determined to be 20 243 Da comprising a sugar moiety of 1865 Da, corresponding to a high mannose-type glycan structure. Due to the high homology among all characterized ABPs, the information on the disulfide bonds will be important for functional analysis of recombinantly expressed ABP1. |
| Databáze: | OpenAIRE |
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