The Isolation and Characterization of Low Molecular Weight Hydrophobic Salt-Soluble Proteins from Barley
- 1 December 1982
- journal article
- research article
- Published by Oxford University Press (OUP) in Journal of Experimental Botany
- Vol. 33 (6), 1325-1331
- https://doi.org/10.1093/jxb/33.6.1325
Abstract
The four main components of the previously designated A-hordein fraction have been purified to homogeneity and partially characterized. Their amino acid composition and solubility properties clearly differ from those of both prolamins and other purified salt-soluble proteins from barley endosperm. Evidence is presented of their homology with the previously described CM-proteins from wheat so their designation as CMa, CMb, CMc and CMd is proposed.This publication has 6 references indexed in Scilit:
- Two Groups of Low Molecular Weight Hydrophobic Proteins from Barley EndospermJournal of Experimental Botany, 1981
- The A-hordeins as a group of salt soluble hydrophobic proteinsPlant Science Letters, 1980
- How reliably do amino acid composition comparisons predict sequence similarities between proteins?Journal of Theoretical Biology, 1979
- Heterogeneity of avenin, the oat prolaminBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Peptide mapping of the major components of in vitro synthesized barley hordein: Evidence of structural homologyCarlsberg Research Communications, 1978
- Relationships among low MW hydrophobic proteins from wheat endospermPhytochemistry, 1978