PURIFICATION OF ADENYLATE KINASE FROM GREEN LEAVES OF BARLEY, MAIZE AND CHENOPODIUM-RUBRUM L

Adenylate kinase (ATP:AMP phosphotransferase, E.C. 2.7.4.3) plays an i mportant role in the regulation of energy metabolism in all living sys tems. The enzyme has been purified and crystallized from a variety of animals and microorganisms, while purification from plant tissues was described only for leaves from the C-4-plant maize. Here, we present a n efficient purification procedure for adenylate kinase derived from g reen leaves of the C-3-plant barley (Hordeum vulgare L.). The same pur ification procedure was applied to adenylate kinases from leaves of ma ize (Zea mays L.) and Chenopodium rubrum. In both these cases, isoform s of adenylate kinase could be purified using an additional affinity c hromatography step. The main isoforms of adenylate kinase from all thr ee plants exhibited apparent molecular masses between 25 and 31 kDa ac cording to gel electrophoresis and gel filtration.