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Titolo:
A SERINE-PROTEASE FROM SUSPENSION-CULTURED SOYBEAN CELLS
Autore:
GUO ZJ; LAMB C; DIXON RA;
Indirizzi:
SAMUEL ROBERTS NOBLE FDN INC,DIV PLANT BIOL,POB 2180 ARDMORE OK 73402 SAMUEL ROBERTS NOBLE FDN INC,DIV PLANT BIOL ARDMORE OK 73402 SALK INST BIOL STUDIES,PLANT BIOL LAB LA JOLLA CA 92037
Titolo Testata:
Phytochemistry
fascicolo: 4, volume: 47, anno: 1998,
pagine: 547 - 553
SICI:
0031-9422(1998)47:4<547:ASFSSC>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROCESSING ENDOPROTEASES; PROLYL ENDOPEPTIDASE; PLASMA-MEMBRANES; TOBACCO PLANTS; GENE; TOMATO; EXPRESSION; SUBTILISIN; PRECURSOR; BINDING;
Keywords:
GLYCINE MAX; LEGUMINOSAE; SERINE PROTEASE; PLANT DEFENSE RESPONSES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
Z.J. Guo et al., "A SERINE-PROTEASE FROM SUSPENSION-CULTURED SOYBEAN CELLS", Phytochemistry, 47(4), 1998, pp. 547-553

Abstract

A serine protease was purified from suspension-cultured soybean cells, by a combination of anion exchange, hydrophobic interaction and affinity chromatography. A 90 000 M-r subunit, which could be photoaffinity labelled with H-3-diisopropylfluorophosphate (DFP), was identified by SDS-polyacrylamide gel electrophoresis. The enzyme had a broad pH optimum from 5.5 to 8.5, and was strongly inhibited by antipain, leupeptin, aminoethytbenzenesulphonyl fluoride (AEBSF) and DFP, but not by soybean trypsin inhibitor. It cleaved several peptide 4-methylcoumaryl-7-amide derivatives after arginine or lysine residues. Mass spectroscopic analysis of oligopeptide digestion products indicated that the preferred cleavage positions were between paired arginine residues, or C-terminal to single arginine residues, depending on the oligopeptide substrate. Partial amino acid sequences from the purified protein showed sequence identity to bacterial protease II and prolyl peptidase, although the enzyme lacked prolyl endopeptidase activity. We discuss the possible involvement of the protease in plant defense responses. (C) 1997 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 22:06:45