Glutathione and superoxide dismutase redox enzyme system during development of toxicoinfectious shock caused by murine plague toxin

1990 ◽  
Vol 109 (2) ◽  
pp. 191-194 ◽  
Author(s):  
N. I. Osipova ◽  
T. D. Cherkasova ◽  
M. Yu. Girshovich ◽  
V. P. Avrorov ◽  
V. Yu. Yurkiv
Planta ◽  
1978 ◽  
Vol 140 (3) ◽  
pp. 221-225 ◽  
Author(s):  
Luís A. del Río ◽  
Francisca Sevilla ◽  
Manuel Gómez ◽  
Juan Yañez ◽  
Julio López

1988 ◽  
Vol 20 (4) ◽  
pp. 377-384 ◽  
Author(s):  
Dianne Fahselt

AbstractThalli of five species of epiphytic lichens were collected from one moribund spruce-fir stand in the Algonquin Highlands in Ontario, Canada. Extracts of all were subjected to isoelectric focusing and stained for activity of 16 enzyme systems. Gels were scored for the presence or absence of individual bands in each enzyme system, and the degree of polymorphism of all detectable enzymes was evaluated using a variability measure developed for use with presence/absence data. Esterase and alkaline phosphatase showed the greatest amount of polymorphism and superoxide dismutase was the least variable enzyme system. The degree of enzyme variability in each of the five species was probably a reflection of its past evolutionary history and bore little relationship to apparent potential for sexual reproduction.


1982 ◽  
Vol 24 (3) ◽  
pp. 325-335 ◽  
Author(s):  
Y. A. El-Kassaby ◽  
F. C. Yeh ◽  
O. Sziklai

The inheritance of 27 loci from 18 enzyme systems was investigated using both megagametophyte and embryo tissues of open pollinated seed collected from a natural stand of coastal Douglas-fir [Pseudotsuga menziesii var. menziesii (Mirb.) Franco]. Four enzyme systems - glutamate dehydrogenase (GDH), glyceraldehyde-3-phosphate dehydrogenase (GAPDH), mannose-6-phosphate isomerase (MPI), and peptidase (PEP) - appeared to be monomorphic and the remaining 14 systems - acid phosphatase (APH), aconitase (ACO), aspartate aminotransferase (AAT), diaphorase (DIA), esterase (EST), glucose-6-phosphate dehydrogenase (G6P), hexoseaminidase (HA), isocitrate dehydrogenase (IDH), malate dehydrogenase (MDH), malic enzyme (ME), phosphoglucose isomerase (PGI), phosphoglucomutase (PGM), 6-phosphogluconic dehydrogenase (6-PGD), and superoxide dismutase (SOD)-showed polymorphism. Each enzyme system was discussed with respect to its multilocus organization, subunit (quaternary) structure, and allelic variation.


2011 ◽  
Vol 183-185 ◽  
pp. 99-103
Author(s):  
Tong Bao ◽  
Li Na Sun ◽  
Qing Hua Xue

Corn (Zea Mays L.) seedlings were in four cadmium (Cd) levels of 0-1mg/L in a hydroponic system to analyze the antioxidant enzyme system, Cd content in the shoots and roots and growth responces in the leaves of corn. There was a significant increase in malondialdehyde (MDA) concentration from Cd 0mg/L to 1mg/L, and peroxidase (POD) and catalase (CAT) activities in the leaves of corn subjected to 0-1mg/L Cd. However there was a significant decrease in superoxide dismutase (SOD) activities subjected to 0-1mg/L Cd. This indicated that Cd stress induced an oxidative stress response in corn seedlings, characterized by an accumulation of MDA, decrease in activities of SOD and increase in activities of POD and CAT. Root and leaf Cd contents of corn increased with their exposure Cd level, and the highest Cd concentration occurred in roots, followed by leaves.


Author(s):  
Jay W. Cha ◽  
Perry J. Melnick

Hereditary ochronosis in very few cases has been examined electron microscopically or histochemically. In this disease homogentisic acid, a normal intermediary of tyrosine metabolism, forms in excessive amounts. This is believed to be due to absence or defective activity of homogentisic acid oxidase, an enzyme system necessary to break the benzene ring and to further break it down to fumaric and acetoacetic acids. Ochronotic pigment, a polymerized form of homogentisic acid, deposits mainly in mesenchymal tissues. There has been a question whether the pigment originates from the collagenous tissues, or deposits passively, where in contrast to melanin it induces degenerative changes.


1994 ◽  
Vol 90 (2) ◽  
pp. 339-347 ◽  
Author(s):  
Maria S. Almansa ◽  
Luis A. del Rio ◽  
Francisca Sevilla

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