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.

Biochemical evidence for the presence of a bifunctional dihydrofolate reductase-thymidylate synthase in plant species / Balestrazzi Alma; Branzoni Manuela; Carbonera Daniela; Parisi Bruno; Cella Rino. - In: JOURNAL OF PLANT PHYSIOLOGY. - ISSN 0176-1617. - STAMPA. - 147(1995), pp. 263-266.

Biochemical evidence for the presence of a bifunctional dihydrofolate reductase-thymidylate synthase in plant species

BALESTRAZZI, ALMA;CARBONERA, DANIELA;CELLA, RINO
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.
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11571/138111
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