Differential alcohol dehydrogenase and malate dehydrogenase isozyme expression in long-term callus tissue cultures ofCereus peruvianus (Cactaceae)

1995 ◽  
Vol 33 (11-12) ◽  
pp. 389-399 ◽  
Author(s):  
E. F. B. Torquato ◽  
A. J. Prioli ◽  
M. F. P. S. Machado
Keyword(s):  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Callus Tissue ◽  
Tissue Cultures ◽  
Dehydrogenase Isozyme

Reptilian alcohol dehydrogenase: Isozyme divergence among submammalian vertebrates

1992 ◽  
Vol 11 (4) ◽  
pp. 412-412
Author(s):  
Lars Hjelmqvist ◽  
Jawed Shafqat ◽  
Hans Jörnvall
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Isozyme

scholarly journals An Alcohol Dehydrogenase 3 (ADH3) from Entamoeba histolytica Is Involved in the Detoxification of Toxic Aldehydes

2020 ◽  
Vol 8 (10) ◽  
pp. 1608
Author(s):  
Constantin König ◽  
Martin Meyer ◽  
Corinna Lender ◽  
Sarah Nehls ◽  
Tina Wallaschkowski ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Entamoeba Histolytica ◽  
Biochemical Characterization ◽  
Stop Codon ◽  
In Silico Analysis ◽  
Peptidase Activity ◽  
Stool Samples ◽  
Human Stool

Recently, a putative alcohol dehydrogenase 3, termed EhADH3B of the Entamoeba histolytica isolate HM-1:IMSS was identified, which is expressed at higher levels in non-pathogenic than in pathogenic amoebae and whose overexpression reduces the virulence of pathogenic amoebae. In an in silico analysis performed in this study, we assigned EhADH3B to a four-member ADH3 family, with ehadh3b present as a duplicate (ehadh3ba/ehadh3bb). In long-term laboratory cultures a mutation was identified at position 496 of ehadh3ba, which codes for a stop codon, which was not the case for amoebae isolated from human stool samples. When using transfectants that overexpress or silence ehadh3bb, we found no or little effect on growth, size, erythrophagocytosis, motility, hemolytic or cysteine peptidase activity. Biochemical characterization of the recombinant EhADH3Bb revealed that this protein forms a dimer containing Ni2+ or Zn2+ as a co-factor and that the enzyme converts acetaldehyde and formaldehyde in the presence of NADPH. A catalytic activity based on alcohols as substrates was not detected. Based on the results, we postulate that EhADH3Bb can reduce free acetaldehyde released by hydrolysis from bifunctional acetaldehyde/alcohol dehydrogenase-bound thiohemiacetal and that it is involved in detoxification of toxic aldehydes produced by the host or the gut microbiota.

Inducing effect of plant cells on nitrogenase activity by Spirillum and Rhizobium in vitro

1978 ◽  
Vol 24 (2) ◽  
pp. 143-148 ◽  
Author(s):  
J. J. Child ◽  
W. G. W. Kurz
Keyword(s):  
Plant Cell ◽  
Callus Tissue ◽  
Nitrogenase Activity ◽  
Nutritional Requirement ◽  
Tissue Cultures ◽  
Cell Tissue ◽  
Direct Association ◽  
Pentose Sugar ◽  
Rhizobium Sp

Eleven different plant cell tissue cultures of both legume and non-legume origin have been grown in direct association, and in separate but close proximal association with both Spirillum lipoferum and Rhizobium sp. 32H1. Basic similarities were found in the nutritional requirement for the induction of nitrogenase activity (C2H2) in both organisms. In the absence of plant cell cultures both organisms need to be provided with a pentose sugar and a tricarboxylic acid to induce high levels of nitrogen-fixing activity. Plant cell callus tissue appears only capable of supplying the tricarboxylic acids needed but not the sugar component. The plant tissue, however, seems able to activate certain carbohydrates, which in themselves are incapable of substituting for the pentose additive.

Hydroxyrutacridon-Epoxid, ein neues Acridon-Alkaloid aus Ruta graveolens / Hydroxyrutacridone Epoxide, a New Acridone Alkaloid from Ruta graveolens

1982 ◽  
Vol 37 (1-2) ◽  
pp. 132-133 ◽  
Author(s):  
U. Eilert ◽  
B. Wolters ◽  
A. Nahrstedt ◽  
V. Wray
Keyword(s):  
Callus Tissue ◽  
Spectroscopic Methods ◽  
Tissue Cultures ◽  
Ruta Graveolens ◽  
Acridone Alkaloid

AbstractHydroxyrutacridone epoxide was isolated from roots and callus tissue cultures of Ruta graveolens L. and identified by spectroscopic methods by comparison to rutacridone epoxide.

Isozymes of amylase, alcohol dehydrogenase, malic enzyme, malate dehydrogenase, and superoxide dismutase in Chloealtis conspersa (Orthoptera)

Genome ◽  
1989 ◽  
Vol 32 (4) ◽  
pp. 596-600 ◽  
Author(s):  
Peter B. Moens ◽  
Steven Kolodziejczyk
Keyword(s):  
Superoxide Dismutase ◽  
Alcohol Dehydrogenase ◽  
Malate Dehydrogenase ◽  
X Chromosome ◽  
Gel Electrophoresis ◽  
Malic Enzyme ◽  
Duplicate Genes ◽  
Gene Linkage ◽  
Slow Band

Five enzymes of the grasshopper Chloealtis conspersa were studied for possible gene linkage. Because of the extreme localization of chiasmata throughout most of the genome of C. conspersa, it was expected that genes would appear either to be completely linked or to assort independently. Our results indicate that malic enzyme and alcohol dehydrogenase are probably on the X chromosome. Superoxide dismutase is produced from the product of duplicate genes where Sod 1-1 is monomorphic and Sod 1-2 has two alleles, one producing a fast-migrating band on gel electrophoresis and one a slow band. While amylase, malate dehydrogenase, and superoxide dismutase appeared to be autosomal, there was no evidence of linkage between them.Key words: Chloealtis conspersa, amylase, alcohol dehydrogenase, malic enzyme, malate dehydrogenase, superoxide dismutase.

Shoot production from onion callus tissue cultures

1978 ◽  
Vol 9 (2) ◽  
pp. 99-110 ◽  
Author(s):  
D.I. Dunstan ◽  
K.C. Short
Keyword(s):  
Callus Tissue ◽  
Tissue Cultures ◽  
Shoot Production
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