0000000001207816

AUTHOR

B. L. Jones

showing 1 related works from this author

Differential localization of two acid proteinases in germinating barley (Hordeum vulgare) seed

1995

A cathepsin D-like aspartic proteinase (EC 3.4.23) is abundant in ungerminated barley (Hordeum vulgare) seed while a 30 kDa cysteine endoproteinase (EC 3.4.22) is one of the proteinases synthesized de novo in the germinating seed. In this work, the localization of these two acid proteinases was studied at both the tissue and subcellular levels by immunomicroscopy. The results confirm that they have completely different functions. The aspartic proteinase was present in the ungerminated seed and, during germination, it appeared in all the living tissues of the grain, including the shoot and root. Contrary to previous suggestions, it was not observed in the starchy endosperm. By immunoblotting…

chemistry.chemical_classificationMolecular massPhysiologyImmunoelectron microscopyfood and beveragesCell BiologyPlant ScienceGeneral MedicineScutellumBiologyEndospermchemistryBiochemistryAleuroneGeneticsStorage proteinHordeum vulgareCysteinePhysiologia Plantarum
researchProduct