Twenty species of seaweed were collected from the coast of Zhejiang, China, extracted with ethanol, and screened for algicidal activity against red tide microalgae H eterosigma akashiwo and Prorocentrum micans. Inhibi...Twenty species of seaweed were collected from the coast of Zhejiang, China, extracted with ethanol, and screened for algicidal activity against red tide microalgae H eterosigma akashiwo and Prorocentrum micans. Inhibitory eff ects of fresh and dried tissues of green alga U lva intestinalis were assessed and the main algicidal compounds were isolated, purifi ed, and identifi ed. Five seaweed species, U. intestinalis, U. fasciata, Grateloupia romosissima, Chondria crassicaulis, and Gracilariopsis lemaneiformis, were investigated for their algicidal activities. Fresh tissues of 8.0 and 16.0 mg/m L of U. intestinalis dissolved in media signifi cantly inhibited growth of H. akashiwo and P. micans, respectively. Dried tissue and ethyl acetate(Et OAc) extracts of U. intestinalis at greater than 1.2 and 0.04 mg/m L, respectively, were fatal to H. akashiwo, while its water and Et OAc extracts in excess of 0.96 and 0.32 mg/m L, respectively, were lethal to P. micans. Three algicidal compounds in the Et OAc extracts were identifi ed as 15-ethoxy-(6z,9z,12z)-hexadecatrienoic acid(I),(6E,9E,12E)-(2-acetoxy- β- D-glucose)-octadecatrienoic acid ester(II) and hexadecanoic acid(III). Of these, compound II displayed the most potent algicidal activity with IC_(50) values of 4.9 and 14.1 μg/m L for H. akashiwo and P. micans, respectively. Compound I showed moderate algicidal activity with IC_(50) values of 13.4 and 24.7 μg/m L for H. akashiwo and P. micans, respectively. These fi ndings suggested that certain macroalgae or products therefrom could be used as ef fective biological control agents against red tide algae.展开更多
Analysis of the mitochondrial proteome would provide valuable insight into the function of this important organelle, which plays key roles in energy metabolism, apoptosis, free radical production, thermogenesis, and c...Analysis of the mitochondrial proteome would provide valuable insight into the function of this important organelle, which plays key roles in energy metabolism, apoptosis, free radical production, thermogenesis, and calcium signaling. It could also increase our understanding about the mechanisms that promote mitochondrial disease. To identify proteins that are antigenically dominant in human liver mitochondria, we generated >240 hybridoma cell lines from native mitochondrial proteins after cell fusion, screening, and cloning. Antibodies that recognized mitochondrial proteins were identified by screening human liver cDNA expression libraries. In this study, we identified 6 major antigens that were recognized by at least 2 different monoclonal antibodies (mAbs). The proteins that were antigenically dominant were: acetyl-Coenzyme A acyltransferase 2 (mitochondrial 3-oxoacyl-Coenzyme A thiolase), aldehyde dehydrogenase 1 family member A1, carbamoyl phosphate synthetase 1, dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex), enoyl coenzyme A hydratase 1, and hydroxysteroid (11-beta) dehydrogenase 1. We also determined the subcellular localizations of these enzymes within the mitochondria using immunohistocytochemistry. We believe that these well-characterized antibodies will provide a valuable resource for the Human Liver Proteome Project (HLPP), and will make studies aimed at investigating liver mitochondrial function far easier to perform in future. Our results provide strong evidence that, (i) depletion of dominant proteins from liver mitochondrial samples is possible and, (ii) the approaches adopted in this study can be used to explore or validate protein-protein interactions in this important organelle.展开更多
基金Supported by the National Natural Science Foundation of China(Nos.40876073,41276122)the Doctoral Fund of the Ministry of Education(No.20123305110002)the K.C.Wong Magna Fund from Ningbo University
文摘Twenty species of seaweed were collected from the coast of Zhejiang, China, extracted with ethanol, and screened for algicidal activity against red tide microalgae H eterosigma akashiwo and Prorocentrum micans. Inhibitory eff ects of fresh and dried tissues of green alga U lva intestinalis were assessed and the main algicidal compounds were isolated, purifi ed, and identifi ed. Five seaweed species, U. intestinalis, U. fasciata, Grateloupia romosissima, Chondria crassicaulis, and Gracilariopsis lemaneiformis, were investigated for their algicidal activities. Fresh tissues of 8.0 and 16.0 mg/m L of U. intestinalis dissolved in media signifi cantly inhibited growth of H. akashiwo and P. micans, respectively. Dried tissue and ethyl acetate(Et OAc) extracts of U. intestinalis at greater than 1.2 and 0.04 mg/m L, respectively, were fatal to H. akashiwo, while its water and Et OAc extracts in excess of 0.96 and 0.32 mg/m L, respectively, were lethal to P. micans. Three algicidal compounds in the Et OAc extracts were identifi ed as 15-ethoxy-(6z,9z,12z)-hexadecatrienoic acid(I),(6E,9E,12E)-(2-acetoxy- β- D-glucose)-octadecatrienoic acid ester(II) and hexadecanoic acid(III). Of these, compound II displayed the most potent algicidal activity with IC_(50) values of 4.9 and 14.1 μg/m L for H. akashiwo and P. micans, respectively. Compound I showed moderate algicidal activity with IC_(50) values of 13.4 and 24.7 μg/m L for H. akashiwo and P. micans, respectively. These fi ndings suggested that certain macroalgae or products therefrom could be used as ef fective biological control agents against red tide algae.
基金supported by the National Basic Research Program of China (Grant No. 2006CB910803)the National High Technology Research and Development Program of China (Grant No. 2006AA02A311)
文摘Analysis of the mitochondrial proteome would provide valuable insight into the function of this important organelle, which plays key roles in energy metabolism, apoptosis, free radical production, thermogenesis, and calcium signaling. It could also increase our understanding about the mechanisms that promote mitochondrial disease. To identify proteins that are antigenically dominant in human liver mitochondria, we generated >240 hybridoma cell lines from native mitochondrial proteins after cell fusion, screening, and cloning. Antibodies that recognized mitochondrial proteins were identified by screening human liver cDNA expression libraries. In this study, we identified 6 major antigens that were recognized by at least 2 different monoclonal antibodies (mAbs). The proteins that were antigenically dominant were: acetyl-Coenzyme A acyltransferase 2 (mitochondrial 3-oxoacyl-Coenzyme A thiolase), aldehyde dehydrogenase 1 family member A1, carbamoyl phosphate synthetase 1, dihydrolipoamide S-acetyltransferase (E2 component of pyruvate dehydrogenase complex), enoyl coenzyme A hydratase 1, and hydroxysteroid (11-beta) dehydrogenase 1. We also determined the subcellular localizations of these enzymes within the mitochondria using immunohistocytochemistry. We believe that these well-characterized antibodies will provide a valuable resource for the Human Liver Proteome Project (HLPP), and will make studies aimed at investigating liver mitochondrial function far easier to perform in future. Our results provide strong evidence that, (i) depletion of dominant proteins from liver mitochondrial samples is possible and, (ii) the approaches adopted in this study can be used to explore or validate protein-protein interactions in this important organelle.
