Purification and characterization of pea chloroplastic phosphoriboisomerase

Pea (Pisum sativum L.) chloroplastic phosphoriboisomerase (EC 5.3.1.6) can be purified to apparent homogeneity in less than 2 days time with a 53% yield. Important steps in the purification include heat treatment and pseudoaffinity chromatography on Red H-3BN Sepharose. The purified isomerase has a...

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Bibliographic Details
Published in:	Plant physiology (Bethesda) Vol. 97; no. 2; pp. 730 - 735
Main Authors:	SKURKRUD, C. L, GORDON, I. M, DORWIN, S, XIAO-HUA YUAN, JOHANSSON, G, ANDERSON, L. E
Format:	Journal Article
Language:	English
Published:	Rockville, MD American Society of Plant Physiologists 01-10-1991
Subjects:	actividad enzimatica activite enzymatique Biological and medical sciences biosintesis biosynthese biosynthesis cetosas chemical composition chloroplaste Chloroplasts ciclo de pentosa fosfato cloroplasto composicion quimica composition chimique cycle du pentose phosphate Dehydrogenases Enzymes enzymic activity fosfatos Fundamental and applied biological sciences. Psychology Gels isomerasas isomerase isomerases ketose ketoses Kinetics Metabolism Peas pentose phosphate cycle phosphate Phosphates pisum sativum Plant physiology and development Plants Proteins purificacion purification Spinach Characterization Ribosephosphate isomerase Purification Leguminosae Vegetable crop Enzymatic activity Enzyme Dicotyledones Pisum sativum Angiospermae Spermatophyta Chloroplast
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Summary:	Pea (Pisum sativum L.) chloroplastic phosphoriboisomerase (EC 5.3.1.6) can be purified to apparent homogeneity in less than 2 days time with a 53% yield. Important steps in the purification include heat treatment and pseudoaffinity chromatography on Red H-3BN Sepharose. The purified isomerase has a subunit molecular mass of 26.4 kD. The N-terminal sequence has been determined through 34 residues. pH optima are 7.8 (ribose-5-phosphate). and 7.7 (ribulose-5-phosphate); Km values are 0.9 millimolar (ribose-5-phosphate) and 0.6 millimolar (ribulose-5-phosphate). The enzyme is inhibited by erythrose-4-phosphate, sedoheptulosebisphosphate, glyceraldehyde-3-phosphate, and 3-phosphoglycerate at concentrations close to those found in photosynthesizing chloroplasts. Countercurrent phase partitioning experiments indicate that the pea chloroplastic phosphoriboisomerase interacts physically with phosphoribulokinase.
Bibliography:	F60 F ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0032-0889 1532-2548
DOI:	10.1104/pp.97.2.730