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Isozymes of pectinesterase and polygalacturonase from Botrytis cinerea Pers
Year:
1988
Source of publication :
Methods in Enzymology
Authors :
Marcus, Lionel
;
.
Volume :
161
Co-Authors:
Schejter, A.
Marcus, L.
Facilitators :
From page:
366
To page:
373
(
Total pages:
8
)
Abstract:
The enzymes pectinesterase and polygalacturonase are secreted by the fungus Botrytis cinerea Pers. and are involved in the rotting and maceration of fresh fruit and vegetables. This enzyme has been purified from fruits and bacteria. This chapter describes assay method and purification procedures for isozymes of Pectinesterase and Polygalacturonase from Botrytis cinerea Pers. The enzyme activity is measured by continuous automatic titration with NaOH of the carboxyl groups released during the reaction. The chapter also describes the properties of the purified isoenzymes. Pectinesterases I and II have molecular weights of 28,400 and 27,800, respectively, by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and 28,100 and 27,600, respectively, by gel exclusion chromatography. The two isoenzymes migrate as single bands in SDS gel electrophoresis. © 1988, Elsevier Inc. All rights reserved.
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DOI :
10.1016/0076-6879(88)61042-1
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
24378
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:06
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Scientific Publication
Isozymes of pectinesterase and polygalacturonase from Botrytis cinerea Pers
161
Schejter, A.
Marcus, L.
Isozymes of pectinesterase and polygalacturonase from Botrytis cinerea Pers
The enzymes pectinesterase and polygalacturonase are secreted by the fungus Botrytis cinerea Pers. and are involved in the rotting and maceration of fresh fruit and vegetables. This enzyme has been purified from fruits and bacteria. This chapter describes assay method and purification procedures for isozymes of Pectinesterase and Polygalacturonase from Botrytis cinerea Pers. The enzyme activity is measured by continuous automatic titration with NaOH of the carboxyl groups released during the reaction. The chapter also describes the properties of the purified isoenzymes. Pectinesterases I and II have molecular weights of 28,400 and 27,800, respectively, by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and 28,100 and 27,600, respectively, by gel exclusion chromatography. The two isoenzymes migrate as single bands in SDS gel electrophoresis. © 1988, Elsevier Inc. All rights reserved.
Scientific Publication
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