The disulfide bond pairing of the pheromones Er‐1 and Er‐2 of the ciliated protozoan Euplotes raikovi

The disulfide pairings of the two Euplotes raikovi pheromones Er‐1 and Er‐2 have been determined by chemical and mass spectrometric analyses. Cystine‐linked peptides from thermolytic digestions of the native molecules were purified by reverse‐phase high performance liquid chromatography and identifi...

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Bibliographic Details
Published in:Protein science 1992-06, Vol.1 (6), p.777-785
Main Authors: Stewart, Albert E., Raffioni, Simona, Bradshaw, Ralph A., Chaudhary, Tanuja, Chait, Brian T., Luporini, Pierangelo
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Biochemistry & Molecular Biology
Chromatography, High Pressure Liquid
Cystine
Disulfides - analysis
Euplotes - physiology
evolution
Life Sciences & Biomedicine
Mass Spectrometry
mass spectroscopy
Membrane Proteins - chemistry
Molecular Sequence Data
Peptide Fragments - isolation & purification
Pheromones - chemistry
polypeptide hormones
Protein Conformation
Protozoan Proteins - chemistry
Science & Technology
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Summary:The disulfide pairings of the two Euplotes raikovi pheromones Er‐1 and Er‐2 have been determined by chemical and mass spectrometric analyses. Cystine‐linked peptides from thermolytic digestions of the native molecules were purified by reverse‐phase high performance liquid chromatography and identified in the known sequences to make the assignments. The same pairing, Cys(I)–Cys(IV), Cys(II)–Cys(VI), and Cys(III)–Cys(V), was found in both pheromones, suggesting that this pattern occurs commonly throughout this family of molecules. This arrangement of disulfides indicates that the three‐dimensional structure is defined by three loops, which can vary in size and charge distribution from one pheromone to another.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560010609