| Title: | Primary structure of the mating pheromone Er-1 of the ciliate Euplotes raikovi |
| Author(s): | Raffioni S; Luporini P; Chait BT; Disper SS; Bradshaw RA; |
| Address: | "Department of Biological Chemistry, California College of Medicine, University of California, Irvine 92717" |
| ISSN/ISBN: | 0021-9258 (Print) 0021-9258 (Linking) |
| Abstract: | "The complete amino acid sequence of the mating pheromone Er-1 purified from Euplotes raikovi homozygous for mat-1 was determined by automated Edman degradation of the whole protein and peptides generated by cyanogen bromide, trypsin, Staphylococcus aureus V8 protease, and chymotrypsin. The proposed sequence is: Asp-Ala-Cys-Glu-Gln-Ala-Ala-Ile-Gln-Cys-Val-Glu-Ser-Ala-Cys-Glu-Ser-Leu- Cys-Thr-Glu-Gly-Glu-Asp-Arg-Thr-Gly-Cys-Tyr-Met-Tyr-Ile-Tyr-Ser-Asn-Cys- Pro-Pro-Tyr-Val The calculated molecular weight is 4411.0, which is in agreement with the averaged mass of 4410.2 obtained by fission fragment ionization mass spectrometry. Previously reported values of the native molecular weight, determined by gel filtration, have ranged from 9,000 to 12,000. Thus, the native structure is likely a dimer (or larger aggregate) of identical subunits with the three disulfide bonds present occurring as intrachain links. Secondary structure predictions suggest a helical structure at the amino terminus. A comparison of the Er-1 amino acid sequence with known protein sequences did not reveal any significant similarities" |
| Keywords: | "Amino Acid Sequence Animals Chromatography, High Pressure Liquid Ciliophora/*physiology Cyanogen Bromide *Membrane Proteins Molecular Sequence Data Peptide Fragments/isolation & purification *Peptides *Pheromones *Protozoan Proteins Trypsin;" |
| Notes: | "MedlineRaffioni, S Luporini, P Chait, B T Disper, S S Bradshaw, R A eng DK32465/DK/NIDDK NIH HHS/ RR00862/RR/NCRR NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 1988/12/05 J Biol Chem. 1988 Dec 5; 263(34):18152-9" |
