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Titolo:
Thermal stress responses of a sterile mutant of Ulva pertusa (Chlorophyta)
Autore:
Kakinuma, M; Shibahara, N; Ikeda, H; Maegawa, M; Amano, H;
Indirizzi:
Mie Univ, Fac Bioresources, Marine Biochem Lab, Tsu, Mie 5148507, Japan Mie Univ Tsu Mie Japan 5148507 arine Biochem Lab, Tsu, Mie 5148507, Japan Mie Univ, Fac Bioresources, Lab Phycol, Tsu, Mie 5148507, Japan Mie Univ Tsu Mie Japan 5148507 urces, Lab Phycol, Tsu, Mie 5148507, Japan
Titolo Testata:
FISHERIES SCIENCE
fascicolo: 2, volume: 67, anno: 2001,
pagine: 287 - 294
SICI:
0919-9268(200104)67:2<287:TSROAS>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMATE-DEHYDROGENASE; HIGHER-PLANTS; ARABIDOPSIS-THALIANA; NITROGEN ASSIMILATION; GEL-ELECTROPHORESIS; METABOLISM; PROTEINS; THERMOTOLERANCE; PHOTOSYNTHESIS; MITOCHONDRIA;
Keywords:
Chlorophyta; glutamate dehydrogenase; isozyme; stress response; thermal stress; Ulva;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Kakinuma, M Mie Univ, Fac Bioresources, Marine Biochem Lab, Tsu, Mie 5148507, Japan Mie Univ Tsu Mie Japan 5148507 m Lab, Tsu, Mie 5148507, Japan
Citazione:
M. Kakinuma et al., "Thermal stress responses of a sterile mutant of Ulva pertusa (Chlorophyta)", FISHERIES S, 67(2), 2001, pp. 287-294

Abstract

The thermal stress responses of a sterile mutant of the marine alga Ulva pertusa were investigated at 20 degreesC and 30 degreesC. The amounts of thephotosynthetic pigments, beta -carotene, chlorophylls a and b, lutein, neoxanthin, and violaxanthin, were 1.4-2.4 times higher in the 30 degreesC-cultivated alga than in the 20 degreesC-cultivated alga. The free amino acids,asparagine, aspartic acid, glutamine, glutamic acid, glycine, and serine, were abundant in the 20 degreesC-cultivated alga, and increased 1.9-10.5-fold in response to thermal stress (30 degreesC). Total carbon and nitrogen contents also increased in the 30 degreesC-cultivated alga. Sodium dodecylsulfate-polyacrylamide gel electrophoretic patterns of total proteins extracted from both temperature-treated algae showed the increases of 20, 25, and 90 kDa proteins in the 30 degreesC-cultivated alga. Isozyme assays for 20 enzymes showed a different banding pattern only in the case of glutamate dehydrogenase (GDH). Although it was observed that both temperature-treated algae possessed NAD(+)- and NADP(+)-specific GDH, the 30 degreesC-cultivated alga had an additional NADP(+)-specific GDH (NADP-GDH). These results suggest that NADP-GDH compensates for the thermally induced decreases in nitrogen assimilation efficiency and thereby regulates nitrogen metabolism under conditions of temperature stress.

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Documento generato il 01/04/20 alle ore 02:07:51