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- Title
Purification and characterization of aconitase isoforms from etiolated pumpkin cotyledons.
- Authors
de Beills, Luigi; RyujiTsugeki; Alpi, Amedeo; Mikio Nishimura
- Abstract
Although aconitase (EC 4.2.1.3) is involved in the glyoxylate cycle, which is localized in glyoxysomes. we detected very low aconitase activity in glyoxysomal fractions after sucrose gradient centrifugation of extracts prepared from etiolated pumpkin (Cucurbita sp.) cotyledons. Two aconitase isoforms were purified to homogeneity. albeit in low yield, by hydrophobic interaction, hydroxylapatite and anion exchange chromatography. They were designated Aco I and Aco II both were shown to be monomeric proteins of Mr 100000 or 98000 by gel filtration and SDS-PAGE analysis. respectively; isoelectric points were 5.0 and 4.8. respectively. Kinetic studies revealed similarities between Aco I and Aco II. A third aconitase isoform (Aco III) was revea1ed but not purified to homogeneity.
- Subjects
CUCURBITA; EMBRYOLOGY; GLYOXYSOMES; CENTRIFUGATION; CHROMATOGRAPHIC analysis; HYDROXYAPATITE; GEL permeation chromatography; KREBS cycle
- Publication
Physiologia Plantarum, 1993, Vol 88, Issue 3, p485
- ISSN
0031-9317
- Publication type
Article
- DOI
10.1111/j.1399-3054.1993.tb01363.x