The addition of gibberellic acid to isolated aleurone layers of barley (Hordeum vulgare L.) causes the production and secretion of four alpha-amylases. Two of these are stable at pH 3.7 and are not inactivated by ethylenediaminetetraacetate. The other two represent the classical barley alpha-amylases; i.e., they are inactivated at pH 3.7 and by reagents which from complexes with divalent metal ...

The 9-kDa thylakoid polypeptide which in vivo carries the iron-sulfur centers A and B of photosystem I was isolated from barley (Hordeum vulgare L.) and the complete amino acid sequence determined. The polypeptide shows a very high degree of homology with the corresponding polypeptides in other plant species. The polypeptide is not post-translationally processed except for the removal of the N-...

Glycolate oxidase is loosely held by microbodies obtained from etiolated barley (Hordeum vulgare L.) leaves depleted of nitrate. Defined centrifugation conditions cause the complete detachment of the enzyme from the microbodies. Addition of nitrate to these plants brings about a greater retention of glycolate oxidase by the microbodies. Synthesis of a nitrate-induced protein seems to be respons...

Increases in two extracellular peroxidases were observed following inoculation of barley (Hordeum vulgare L.) with the powdery mildew pathogen (Erysiphe graminis DC.: Fr. f. sp. hordei Em. Marchal). The more prominent isozyme, P8.5, was purified from intercellular wash fluids by acetone precipitation, ion-exchange chromatography, isoelectric focusing, and gel filtration. Purified P8.5 is a heme...