Abstract
Three lines of evidence are presented that confirm the sensitivity of the bicinchonic acid protein assay to the content of lysyl residues of proteins. Small samples of barley were extracted with sodium dodecyl sulphate/tris (hydroxymethyl) aminomethane buffer at 60 °C. These extracts were then used in the bicinchonic acid assay. Protein content, based on the UV absorbance of the peptide bond, can be determined from the same extracts without staining. High-lysine barley lines could be distinguished from normal-lysine lines on the basis of these two measurements. The technique can be extended to samples from single half-endosperms thus allowing the embryo-ends to be saved for growing.
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