Adenylate kinase from plant tissues. Influence of ribonuclease on binding properties on Mono Q.
Adenylate kinases modulate the three adenine nucleotide pools and were found to be localized as isoenzymes in different tissues and organelles in animals and plants. For investigations of adenylate kinase isoenzymes from plant tissues different plant extracts were examined by anion-exchange chromatography. During investigations with the strong anion exchanger Mono Q, adenylate kinase activity eluted in the void volume. This void volume activity did not always occur, but depended on the age of the plants and light treatment. The nature of the factors affecting void volume activity could only be partially resolved. It could be shown that RNase treatment at the beginning of extraction led to the disappearance of void volume activity, whereas an untreated extract still showed this activity.
Institut für Biologie II, Universität Freiburg, Germany.
W R
WR
Deppert
J
J
Normann
E
E
Wagner
D000263:Adenylate Kinase / Q000302:isolation & purification* / Q000378:metabolism; D000837:Anion Exchange Resins / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D011485:Protein Binding; D012117:Resins, Synthetic; D012260:Ribonucleases / Q000378:metabolism*
D000837:Anion Exchange Resins; D007527:Isoenzymes; D012117:Resins, Synthetic; C042855:Mono Q; D000263:Adenylate Kinase; D012260:Ribonucleases