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Titolo:
Purification and characterization of Delta(1)-pyrroline-5-carboxylate reductase isoenzymes, indicating differential distribution in spinach (Spinaciaoleracea L.) leaves
Autore:
Murahama, M; Yoshida, T; Hayashi, F; Ichino, T; Sanada, Y; Wada, K;
Indirizzi:
Kanazawa Univ, Fac Sci, Dept Biol, Kanazawa, Ishikawa 9201192, Japan Kanazawa Univ Kanazawa Ishikawa Japan 9201192 wa, Ishikawa 9201192, Japan
Titolo Testata:
PLANT AND CELL PHYSIOLOGY
fascicolo: 7, volume: 42, anno: 2001,
pagine: 742 - 750
SICI:
0032-0781(200107)42:7<742:PACODR>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESEMBRYANTHEMUM-CRYSTALLINUM L; HORDEUM-VULGARE L; PISUM-SATIVUM-L; PYRROLINE-5-CARBOXYLATE REDUCTASE; DELTA-1-PYRROLINE-5-CARBOXYLATE REDUCTASE; PROLINE BIOSYNTHESIS; ARABIDOPSIS-THALIANA; FERREDOXIN ISOPROTEINS; MOLECULAR-CLONING; OSMOTIC-STRESS;
Keywords:
chloroplast; isoenzemes; partial amino acid sequence; proline biosynthesis; Delta(1)-pyrroline-5-carboxylate (P5C); spinach (Spinacia oleracea); water stress;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Wada, K Kanazawa Univ, Fac Sci, Dept Biol, Kanazawa, Ishikawa 9201192, Japan Kanazawa Univ Kanazawa Ishikawa Japan 9201192 kawa 9201192, Japan
Citazione:
M. Murahama et al., "Purification and characterization of Delta(1)-pyrroline-5-carboxylate reductase isoenzymes, indicating differential distribution in spinach (Spinaciaoleracea L.) leaves", PLANT CEL P, 42(7), 2001, pp. 742-750

Abstract

Delta (1)-Pyrroline-5-carboxylate reductase (P5CR) (EC 1.5.1.2. L-proline:NAD(P)-5-oxidoreductase), the second enzyme in the proline biosynthetic pathway, was purified from spinach (Spinacia oleracea L.) leaves. Following ammonium sulfate fractionation, purification was performed by several chromatographic methods: Blue Cellulofine, DEAE-TOYOPEARL, -Sephacryl S-300 HR, and POROS QE/M, Two isoenzymes resolved by anion exchange chromatography were designated P5CR-1 and P5CR-2, Only P5CR-2 was purified from the intact chloroplasts, indicating differential distribution of the isoenzymes, P5CR isoenzymes, P5CR-1 and P5CR-2, are a homopolymer with an apparent molecular mass of 310 kDa, consisting of 10 to 12 subunits of about 28.5 kDa, P5CR-1 and P5CR-2 showed K-m values of 9 and 19 muM for NADPH and values of 0.122 and 0.162 mM for Delta (1)-pyrroline-5-carboxylate (P5C), respectively We decided partial amino acid sequences of PSCR-1 which showed the 70 to 80% homology to the deduced amino acid sequences of several plant P5CR cDNAs. Bothisoenzymes had much lower affinity for NADH than for NADPH and were inhibited by free ATP and Mg2+ ion. The inhibition was partially mitigated when ATP and Mg2+ were added simultaneously to the reaction mixture. Cations at high concentration were inhibitory to P5CR activity, Interestingly, P5CR-2 was more stable to heat treatment at 40 degreesC than P5CR-1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/04/20 alle ore 23:00:44