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Single step chromatographic purification and characterization of the endopolygalacturonases and pectinesterases of the fungus, Botrytis cinerea Pers
Year:
1983
Source of publication :
Physiological Plant Pathology
Authors :
Marcus, Lionel
;
.
Volume :
23
Co-Authors:
Marcus, L., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, 69978, Israel
Schejter, A., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, 69978, Israel
Facilitators :
From page:
1
To page:
13
(
Total pages:
13
)
Abstract:
This communication describes the purification, in a single chromatographic step on cross-linked polypectate, of two pectinesterases and two endopolygalacturonases found inthe extracellular fluid of cultures of the fungus, Botrytis cinerea. The endopolygalacturonases, PG-I and PG-II, have molecular weights of 34 000 and 56 000, respectively. They differ in their chromatographic behaviour, PG-II being more strongly retained by the cross-linked polypectate column. The pectinesterases, PE-I and PE-II, have nearly identical molecular weights of about 28 000 and very similar amino acid compositions, suggesting a common genetic origin. It is shown that Michaelis-Menten behaviour is obeyed by all these enzymes. The enzyme kinetic constants of PG-I and PG-II are strongly dependent on the salt concentration of the medium; both polyglutamate and pectin act as competitive inhibitors. The properties of PE-I and PE-II of B. cinerea are found to be strikingly similar to those of the two pectin-esterases purified from oranges. © 1983.
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DOI :
10.1016/0048-4059(83)90031-0
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
29936
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:50
Scientific Publication
Single step chromatographic purification and characterization of the endopolygalacturonases and pectinesterases of the fungus, Botrytis cinerea Pers
23
Marcus, L., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, 69978, Israel
Schejter, A., Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Ramat Aviv, 69978, Israel
Single step chromatographic purification and characterization of the endopolygalacturonases and pectinesterases of the fungus, Botrytis cinerea Pers
This communication describes the purification, in a single chromatographic step on cross-linked polypectate, of two pectinesterases and two endopolygalacturonases found inthe extracellular fluid of cultures of the fungus, Botrytis cinerea. The endopolygalacturonases, PG-I and PG-II, have molecular weights of 34 000 and 56 000, respectively. They differ in their chromatographic behaviour, PG-II being more strongly retained by the cross-linked polypectate column. The pectinesterases, PE-I and PE-II, have nearly identical molecular weights of about 28 000 and very similar amino acid compositions, suggesting a common genetic origin. It is shown that Michaelis-Menten behaviour is obeyed by all these enzymes. The enzyme kinetic constants of PG-I and PG-II are strongly dependent on the salt concentration of the medium; both polyglutamate and pectin act as competitive inhibitors. The properties of PE-I and PE-II of B. cinerea are found to be strikingly similar to those of the two pectin-esterases purified from oranges. © 1983.
Scientific Publication
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