http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8713
Pectin methylesterase from Kiwi and Kaki fruits: purification, characterization and role of pH in the enzyme regulation and interaction with the Kiwi proteinaceous inhibitor (Articolo in rivista)
- Type
- Label
- Pectin methylesterase from Kiwi and Kaki fruits: purification, characterization and role of pH in the enzyme regulation and interaction with the Kiwi proteinaceous inhibitor (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1021/jf0491963 (literal)
- Alternative label
Ciardiello M.A.; Tamburrini M.; Tuppo L.; Carratore V.; Giovane A.; Mattei B.; Camardella L. (2004)
Pectin methylesterase from Kiwi and Kaki fruits: purification, characterization and role of pH in the enzyme regulation and interaction with the Kiwi proteinaceous inhibitor
in Journal of agricultural and food chemistry
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Ciardiello M.A.; Tamburrini M.; Tuppo L.; Carratore V.; Giovane A.; Mattei B.; Camardella L. (literal)
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- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Institute of Protein Biochemistry, CNR, Via Marconi 12, I-80125 Napoli, Italy,
Department of Biochemistry and Biophysics, II University of Napoli, Via Costantinopoli 16,
I-80138 Napoli, Italy, and Department of Plant Biology, University of Roma \"La Sapienza\",
Piazzale Aldo Moro 5, I-00185 Roma, Italy (literal)
- Titolo
- Pectin methylesterase from Kiwi and Kaki fruits: purification, characterization and role of pH in the enzyme regulation and interaction with the Kiwi proteinaceous inhibitor (literal)
- Abstract
- Pectin methylesterase was purified from kiwi (Actinidia chinensis) and kaki fruit ( Diospyros kaki). The pH values of the fruit homogenates were 3.5 and 6.2, respectively. The kiwi enzyme is localized in the cell wall and has a neutral-alkaline pI, whereas the kaki enzyme is localized in the soluble fraction and has a neutral-acidic pI. The molecular weights of the kiwi and kaki enzymes were 50 and 37 kDa, respectively. The two enzymes showed a similar salt and pH dependence of activity, and a different pH dependence of the inhibition by the kiwi proteinaceous inhibitor. (literal)
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