Biochemical evidence for the presence of a bifunctional dihydrofolate reductase-thymidylate synthase in plant species
Articolo
Data di Pubblicazione:
1995
Abstract:
It is shown that wild carrot cells contain both a bifunctional DHFR-TS (EC 2.1.1.45) and a monofunctional
DHFR (EC 1.5.1.3). The bifunctional protein was present as the major DHFR fraction (80%)
eluted from MTX-Sepharose. SDS-PAGE and immunoblot experiments showed that wild and domesticated
carrot DHFR-TS have the same molecular mass (about 58 kDa). The immunochemical analysis
showed the occurrence of the 58 kDa polypeptide also in the Nicotiana plumbaginifolia MTX-Sepharose
fraction, whereas a band of about 50 kDa was recognized in Oryza sativa. DHFR and TS activities were
present in both purified fractions. These data indicate that the bifunctional DHFR-TS is ubiquitous in
plant cells.
DHFR (EC 1.5.1.3). The bifunctional protein was present as the major DHFR fraction (80%)
eluted from MTX-Sepharose. SDS-PAGE and immunoblot experiments showed that wild and domesticated
carrot DHFR-TS have the same molecular mass (about 58 kDa). The immunochemical analysis
showed the occurrence of the 58 kDa polypeptide also in the Nicotiana plumbaginifolia MTX-Sepharose
fraction, whereas a band of about 50 kDa was recognized in Oryza sativa. DHFR and TS activities were
present in both purified fractions. These data indicate that the bifunctional DHFR-TS is ubiquitous in
plant cells.
Tipologia CRIS:
1.1 Articolo in rivista
Keywords:
Daucus earota; dihydrofolate reduetase-thymidylate synthase; Nieotiana plumbaginifolia (Doba cell line); Oryza sativa; isozymes
Elenco autori:
Balestrazzi, Alma; Branzoni, Manuela; Carbonera, Daniela; Parisi, Bruno; Cella, Rino
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