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Titolo:
Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae)
Autore:
Trejo, SA; Lopez, LMI; Cimino, CV; Caffini, NO; Natalucci, CL;
Indirizzi:
LIPROVE, La Plata, Argentina LIPROVE La Plata ArgentinaLIPROVE, La Plata, Argentina Univ Nacl La Plata, Fac Ciencias Exactas, Dept Ciencias Biol, La Plata, Argentina Univ Nacl La Plata La Plata Argentina iencias Biol, La Plata, Argentina
Titolo Testata:
JOURNAL OF PROTEIN CHEMISTRY
fascicolo: 6, volume: 20, anno: 2001,
pagine: 469 - 477
SICI:
0277-8033(200108)20:6<469:PACOAN>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; CYSTEINE PROTEASE; MULTIPLE FORMS; THIOL PROTEASE; CARICA-PAPAYA; EXPRESSION; PROTEINASE; SENESCENCE; CDNA; GENE;
Keywords:
Asclepias fruticosa; Aselepiadaceae; latex; milkweed; plant endopeptidases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Caffini, NO LIPROVE, CC 711,B1900AVW, La Plata, Argentina LIPROVE CC 711,B1900AVW La Plata Argentina Plata, Argentina
Citazione:
S.A. Trejo et al., "Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae)", J PROTEIN C, 20(6), 2001, pp. 469-477

Abstract

Asclepias fruticosa L. is a small shrub containing latex with proteolytic activity. The crude extract (latex diluted 1:250 and ultracentrifuged) contained 276 mug of protein/mL and the proteolytic activity reached 1.2 caseinolytic U/mL. This enzyme preparation was very stable even after 2 hours at 45 degreesC, but was quickly inactivated after 5 minutes at 80 degreesC. Chromatographic purification was achieved by FPLC using a cation exchanger (SP-Sepharose FF). Thus, a unique proteolitically active fraction could be isolated, being homogeneous by bidimensional electrophoresis and mass spectrometry (M-r = 23,652). The optimum pH range was achieved at 8.5-10.5. The enzyme activity was completely inhibited by specific cysteine peptidases inhibitors. Isoelectric focusing followed by zymogram showed the enzyme had a pI greater than 9.3. The N-terminus sequence (LPDSVD-WREKGVVFPIRNQGK) shows a great deal of similarity to those of the other cysteine endopeptidases isolated from latices of Asclepiadaceae even when a high degree of homology could be observed with other plant cysteine endopeptidases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/11/20 alle ore 03:39:35