Open AccessProperties of Ornithine Carbamoyltransferase from Pisum sativum L
Author(s) -
H. de Ruiter,
C. Kollöffel
Publication year - 1985
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.77.3.695
Subject(s) - pisum , ornithine carbamoyltransferase , sativum , ammonium , ornithine , biochemistry , enzyme , biology , ammonium sulfate , transferase , aspartate carbamoyltransferase , elution , molar concentration , chromatography , chemistry , botany , amino acid , organic chemistry , arginine , allosteric regulation
Some properties of ornithine carbamoyltransferase from chloroplasts isolated from leaves of Pisum sativum L. (cv Marzia) were compared with those of the enzyme partially purified (316-fold) from shoots of seedlings after 3 weeks of cultivation.Both preparations showed a pH optimum at pH 8.3 and had the same affinity to ornithine (K(m) = 1.2 millimolar) as well as to carbamoyl phosphate (K(m) = 0.2 millimolar). The approximate molecular weight determined by gel sieving was 77,600.A desalted ammonium sulfate precipitate from 14-day seedlings (inclusive roots and senescing cotyledons) was applied on a column of anion exchanger. The elution pattern showed one peak of ornithine carbamoyl-transferase activity. This elution pattern was the same as observed for the enzyme from chloroplasts.The results suggest the presence of one form of ornithine carbamoyl-transferase in pea seedlings.