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Zabielski, Piotr ; Strumiło, Sławomir ; Święcicka, Izabela
Publisher:Komitet Biotechnologii PAN ; Instytut Chemii Bioorganicznej PAN
Date issued/created: Subject and Keywords: Abstract:The NADP+ - dependent isocitrate dehydrogenase (IDH) from Bacilluslicheniformis was partially purified using ammonium sulphate fractionation andgel filtration on Sephadex G-200 column. The enzyme preparation had specificactivity of 1.52 U mg ’. The temperature optimum for the IDH activity was about59°C. The Arrthenius activation energy was determined to be 65.3 kj/mol below47°C, and 18.3 kJ/mol above this temperature. The IDH activity at 65°C wasmuch protected by isocitrate and magnesium, but no NADP+. Manganese ionswere more efficient activators ofthe enzyme than Mg^+. Calcium ions rather inhibited the IDH. The Km values for DL-isocitrate and NADP+ in phosphate buffer(pH 7.4) at 20°C were 85.5 and 4.9 pM, respectively: at 58°C the correspondingvalues were 181.5 and 69.3 pM.
Relation:Biotechnologia, vol.54, 3 (2001)-.
Volume: Issue: Start page: End page: Resource type: Detailed Resource Type: Format: Resource Identifier: Source:Biblioteka Instytutu Chemii Bioorganicznej PAN
Language: Language of abstract: Temporal coverage: Rights:Licencja Creative Commons Uznanie autorstwa-Na tych samych warunkach 4.0
Terms of use: Digitizing institution:Instytut Chemii Bioorganicznej Polskiej Akademii Nauk
Original in:Instytut Chemii Bioorganicznej Polskiej Akademii Nauk
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