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Titolo:
CHARACTERIZATION OF MULTIPLE FORMS OF POLYPHENOLOXIDASE FROM APPLE FRUIT
Autore:
MARQUES L; FLEURIET A; MACHEIX JJ;
Indirizzi:
UNIV MONTPELLIER 2,BIOTECHNOL & PHYSIOL VEGETALES APPL LAB,EA 728,PL EUGENE BATAILLON F-34095 MONTPELLIER 05 FRANCE UNIV MONTPELLIER 2,BIOTECHNOL & PHYSIOL VEGETALES APPL LAB,EA 728 F-34095 MONTPELLIER 05 FRANCE CTIFL F-13210 ST REMY PROVENCE FRANCE
Titolo Testata:
Plant physiology and biochemistry
fascicolo: 2, volume: 33, anno: 1995,
pagine: 193 - 200
SICI:
0981-9428(1995)33:2<193:COMFOP>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
VARIEGATED GRAPEVINE MUTANT; CHLOROGENIC ACID OXIDASE; MALUS-PUMILA; PURIFICATION; INHIBITION; PLANTS; MEMBRANE; CLEAVAGE; CLONING; PROTEIN;
Keywords:
POLYPHENOLOXIDASE; APPLE FRUIT; BIOCHEMICAL CHARACTERISTICS; MOLECULAR MASS; DISULFIDE BONDS; PYRUS MALUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
L. Marques et al., "CHARACTERIZATION OF MULTIPLE FORMS OF POLYPHENOLOXIDASE FROM APPLE FRUIT", Plant physiology and biochemistry, 33(2), 1995, pp. 193-200

Abstract

Polyphenoloxidase (PPO) (E.C.1.10.3.1) from apple (Pyrus malus L. cv Granny Smith) pulp thylakoidal membranes presented multiple forms whenseparated under partially denaturing conditions and revealed by Western-blot using apple anti-PPO antibodies: a main active band, a faint active band already described as stable proteolysed form, and a third inactive band. The two active forms were studied for their optimum pH with or without sodium dodecyl sulfate (SDS). The main active PPO was found to have the same activity level at pH 4 (thylakoidal lumen pH) asat pH 6 with SDS, therefore apple PPO does not show any latency. It was shown to acquire a broader range of pH conditions by proteolysis orby SDS addition which might signify that a regulatory domain pH-controls the active site. The estimated molecular mass of the main active and proteolysed forms were respectively 64 and 42 kDa. Denaturation by guanidinium chloride of a native PPO extract led to a single 63-kDa band shifted in a 64-kDa band with reduction by dithiothreitol, indicating that PPO protein contains internal disulfide bonds. This denaturation study led us to suggest that the inactive PPO form present in the native extract may be the partially unfolded PPO translocation-competent form entering thylakoidal membranes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 11:22:12