Premium
Induction of a specific isoenzyme of glutamate dehydrogenase during isolation and the first 48 h of culture of Brassica napus leaf protoplasts
Author(s) -
Watanabe Masami,
Nakayama Hiroyuki,
Watanabe Yukio,
Shimada Noritsugu
Publication year - 1992
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1034/j.1399-3054.1992.860207.x
Subject(s) - glutamate dehydrogenase , protoplast , biology , biochemistry , nad+ kinase , isozyme , polyacrylamide gel electrophoresis , brassica , ammonium , enzyme , microbiology and biotechnology , botany , chemistry , glutamate receptor , receptor , organic chemistry
The specific activity of NADH‐glutamate dehydrogenase (GDH, EC 1.4.1.2) in leaf protoplasts ( Brassica napus L. cv. Bronowski) was initially low and progressively increased during culture in Murashige and Skoog (MS) medium and MS (−NH 4 ) (ammonium nitrate‐free MS) medium in the dark. Native polyacrylamide gel electrophoresis (PAGE) and tetrazolium staining revealed that the high specific activity of NAD‐GDH (deamination) in leaves correlated with the cathodal isoenzymes, and the high specific activity of NADH‐GDH (amination) in leaf protoplasts to the anodal ones. Changes in isoenzyme pattern were correlated with an increase in the specific activity of NADH‐GDH but not with the NADH‐GDH/NAD‐GDH ratio. The increase in NADH‐GDH (amination) activity of leaf protoplasts was correlated with the occurrence of the isoenzyme GDH7, which was not detected in leaves.