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Registro Completo |
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Biblioteca(s): |
Embrapa Soja. |
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Data corrente: |
31/07/1992 |
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Data da última atualização: |
28/03/2012 |
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Autoria: |
ITO, H.; NOBUTSUGU, H.; AKIRA, O.; OHBAYASHI, A.; OHASHI, Y. |
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Afiliação: |
Bioproducts Development Center e Central Research Laboratories, Takara Shuzo Co., Ltd., Seta 3-4-1, Otsu, Shiga 520-21, Japan. |
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Título: |
Purification and characterization of rice peroxidases. |
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Ano de publicação: |
1991 |
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Fonte/Imprenta: |
Agricultural and Biological Chemistry, v.55, n.10, p.2445-2454, 1991. |
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Idioma: |
Inglês |
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Conteúdo: |
Four peroxidase components, named RP-2, 4,6, and 7, were isolated from ice (Oryza sativa L.) green leaves. Isoelectric focusing indicated that each preparation was homogeneours. The molecular weights of RP-2,4,6, and 7 estimated by SDS-PAGE were 48,000, 48,000, 40,000, and 39,500, and their isoelectric points were 5,4, 8,1, 9,3, and 9,2, respectively. The activity of every preparation was maximum around pH 5.0. Antisera against these purified enzymes were raised in rabbits. Ouchterlony double diffusion tests with these antisera suggested that RP-6 and 7 were immunochemically identical and RP-2 and 4 were identical in parts and that RP-6 and 7 were quite different from RP-2 and 4. Analysis of the N-terminal amino acid sequences also showed that these peroxidase components were classified into two groups. The polymerase chain reaction showed that RP-2 and/ or RP-4 contained an active central region, which is homologous to other plant peroxidases. |
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Palavras-Chave: |
Caracterizacao; Characterization; Purification. |
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Thesagro: |
Arroz; Peroxidase; Purificação. |
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Thesaurus Nal: |
rice. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 01605naa a2200253 a 4500
001 1457788
005 2012-03-28
008 1991 bl --- 0-- u #d
100 1 $aITO, H.
245 $aPurification and characterization of rice peroxidases.
260 $c1991
520 $aFour peroxidase components, named RP-2, 4,6, and 7, were isolated from ice (Oryza sativa L.) green leaves. Isoelectric focusing indicated that each preparation was homogeneours. The molecular weights of RP-2,4,6, and 7 estimated by SDS-PAGE were 48,000, 48,000, 40,000, and 39,500, and their isoelectric points were 5,4, 8,1, 9,3, and 9,2, respectively. The activity of every preparation was maximum around pH 5.0. Antisera against these purified enzymes were raised in rabbits. Ouchterlony double diffusion tests with these antisera suggested that RP-6 and 7 were immunochemically identical and RP-2 and 4 were identical in parts and that RP-6 and 7 were quite different from RP-2 and 4. Analysis of the N-terminal amino acid sequences also showed that these peroxidase components were classified into two groups. The polymerase chain reaction showed that RP-2 and/ or RP-4 contained an active central region, which is homologous to other plant peroxidases.
650 $arice
650 $aArroz
650 $aPeroxidase
650 $aPurificação
653 $aCaracterizacao
653 $aCharacterization
653 $aPurification
700 1 $aNOBUTSUGU, H.
700 1 $aAKIRA, O.
700 1 $aOHBAYASHI, A.
700 1 $aOHASHI, Y.
773 $tAgricultural and Biological Chemistry$gv.55, n.10, p.2445-2454, 1991.
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Embrapa Soja (CNPSO) |
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