TAILIEUCHUNG - Báo cáo khoa học: Biochemical characterization of the major sorghum grain peroxidase

The major cationic peroxidase in sorghum grain (SPC4) , which is ubiqui-tously present in all sorghum varieties was purified to apparent homogen-eity, and found to be a highly basic protein (pI 11). MS analysis showed that SPC4 consists of two glycoforms with molecular masses of 34227 and 35629 Da and it contains a type-b heme. | ềFEBS Journal Biochemical characterization of the major sorghum grain peroxidase Mamoudou H. Dicko1 2 3 Harry Gruppen2 Riet Hilhorst1 Alphons G. J. Voragen2 and Willem J. H. van Berkel1 1 Laboratory of Biochemistry Department of Agrotechnology and Food Sciences Wageningen University The Netherlands 2 Laboratory of Food Chemistry Department of Agrotechnology and Food Sciences Wageningen University The Netherlands 3 Laboratoire de Biochimie CRSBAN UFR-SVT Universite de Ouagadougou Burkina Faso Keywords glycoform hemeprotein isoenzyme peroxidase sorghum Correspondence M. H. Dicko Laboratoire de Biochimie CRSBAN UFR-SVT Universite de Ouagadougou 03 BP. 7021 Ouagadougou 03 Burkina Faso Fax 226 50337373 Tel 226 70272643 E-mail mdicko@ W. J. H. van Berkel Laboratory of Biochemistry Department of Agrotechnology and Food Sciences Wageningen University PO Box 8128 6700 ET Wageningen The Netherlands Fax 31 317484801 Tel 31 317482861 E-mail Present address PamGene PO Box 1345 5200 BJ s-Hertogenbosch The Netherlands Database Sequence data for sorghum peroxidase described here has been submitted to the UnitProt knowledgebase under the accession number P84516 The major cationic peroxidase in sorghum grain SPC4 which is ubiquitously present in all sorghum varieties was purified to apparent homogeneity and found to be a highly basic protein pI 11 . MS analysis showed that SPC4 consists of two glycoforms with molecular masses of 34227 and 35629 Da and it contains a type-b heme. Chemical deglycosylation allowed to estimate sugar contents of and w w in glycoform I and II respectively and a mass of the apoprotein of 33 246 Da. High performance anion exchange chromatography allowed to determine the carbohydrate constituents of the polysaccharide chains. The N-terminal sequence of SPC4 is not blocked by pyroglutamate. MS analysis showed that six peptides including the N-terminal sequence of SPC4 matched with the predicted tryptic peptides of .

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