The amino acid sequence of wheat histone H2A(1). A core histone with a C-terminal extension
Open Access
- 1 August 1985
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 150 (3), 499-506
- https://doi.org/10.1111/j.1432-1033.1985.tb09050.x
Abstract
1. The complete amino acid sequence (145 residues) of histone variant H2A(1) from wheat germ Triticum aestivum cultivar T 4 has been established from Edman degradation of large overlapping fragments. 2. The sequence of histone variant H2A(1) differs from the homologous calf histone in 61 amino acid positions. These differences include an extension of H2A(1) by 19 amino acids at its carboxyl end.This publication has 33 references indexed in Scilit:
- A simple modification converts the spinning cup protein sequencer into a vapour‐phase sequencerFEBS Letters, 1984
- Stepwise sequence determination from the carboxyl terminus of peptidesBiochemistry, 1982
- The Primary Structure of Histone H2A from the Sperm Cell of the Sea Urchin Parechinus angulosusEuropean Journal of Biochemistry, 1980
- The Histone H2B from the Sperm Cell of the Starfish Marthasterias glacialisEuropean Journal of Biochemistry, 1980
- More histone structuresFEBS Letters, 1979
- The Complete Amino‐Acid Sequence of Histone H2B(3) from Sperm of the Sea Urchin Parechinus angulosusEuropean Journal of Biochemistry, 1978
- Primary structure of chicken erythrocyte histone H2ABiochimie, 1978
- ChromatinNature, 1978
- The Determination of the Primary Structure of Histone F3 from Chicken Erythrocytes by Automatic Edman DegradationEuropean Journal of Biochemistry, 1974
- Determination of the carboxyl termini of proteins with ammonium thiocyanate and acetic anhydride, with direct identification of the thiohydantoinsBiochemistry, 1969