Immunocharacterization of NADH-Glutamate Dehydrogenase from Vitis vinifera L | Zendy

Constantinos A. Loulakakis | Zendy; Kalliopi A. Roubelakis–Angelakis | Zendy

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Immunocharacterization of NADH-Glutamate Dehydrogenase from Vitis vinifera L

Author(s) -

Constantinos A. Loulakakis,

Kalliopi A. Roubelakis–Angelakis

Publication year - 1990

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.94.1.109

Subject(s) - glutamate dehydrogenase , antiserum , biochemistry , isozyme , shoot , protein subunit , biology , molecular mass , enzyme , ammonium , western blot , lactate dehydrogenase , microbiology and biotechnology , explant culture , in vitro , chemistry , glutamate receptor , botany , gene , antibody , receptor , organic chemistry , immunology

Rabbit antiserum was raised against NADH-glutamate dehydrogenase (GDH) isoenzyme 1, purified from leaves of Vitis vinifera L. cv Soultanina and its specificity was tested. This antiserum was used for immunocharacterization of the GDH from leaf, shoot, and root tissues. The antiserum recognized the seven isoenzymes of NADH-GDH and precipitated all the enzyme activity from the three tissues tested. Western blot following SDS-PAGE revealed the same protein band for the three tissues, with a molecular mass of 42.5 kilodaltons corresponding to NADH-GDH subunit. Results, based on the immunological studies, revealed that NADH-GDH from leaf, shoot, and root tissues are closely related proteins. Furthermore, addition of ammonium ions to the culture medium of in vitro grown explants resulted in a significant increase in NADH-GDH activity in root, shoot, and leaf tissues.

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