scholarly journals A Study of the Glutathione Transferase Proteome of Drosophila melanogaster: Use of S- Substituted Glutathiones as Affinity Ligands

10.5772/35488 ◽  
2012 ◽  
Author(s):  
Ramavati Pal ◽  
Milana Blakemore ◽  
Michelle Ding ◽  
Alan G.
Keyword(s):  
Drosophila Melanogaster ◽  
Glutathione Transferase ◽  
Affinity Ligands

Isolation, Characterization and Comparison of Antipeptide and Antiprotein Rabbit Antibodies to the π-Isoform of Glutathione S-Transferase

1998 ◽  
Vol 53 (9-10) ◽  
pp. 902-910 ◽  
Author(s):  
Francesca Di Modugno ◽  
Laura Rosano ◽  
Mauro Castelli ◽  
Alberto Chersi
Keyword(s):  
Cancer Progression ◽  
Glutathione Transferase ◽  
Solid Phase ◽  
Elisa Test ◽  
Glutathione S Transferase ◽  
Affinity Ligands ◽  
Antipeptide Antibodies ◽  
Binding Data ◽  
Linear Epitopes ◽  
Active Fragments

The main linear epitopes of π-glutathione transferase (π-GST, EC 2.5.1.18), an enzyme related to cancer progression in a restricted number of tumours, were identified by testing in ELISA the reactivities of polyclonal anti-π-GST rabbit sera against a panel of 51 overlapping decapeptides, covering the whole 216-residue sequence of the protein. Several major reactivity peaks were detected, each covering two or three adjacent peptides. The most active fragments were then reconstructed by conventional solid-phase synthesis, linked to Sepharose, and used as affinity ligands for isolating specific anti-π-GST antibody subsets. A second group of antisera was then prepared in rabbits by using as immunogens some of the above described synthetic fragments, linked to a carrier protein, and antipeptide antibodies purified by affinity chromatography. An ELISA test was then performed, using as antigens a panel of peptides and different isoforms of GST, in order to establish whether antibodies isolated from total anti-π-GST sera would display higher reactivity and specificity, as compared to traditional antipeptide antibodies. Binding data clearly confirm that the formers might be indeed better reagents for the detection and possibly quantitation of π-GST.

A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster

2012 ◽  
Vol 442 (1) ◽  
pp. 181-190 ◽  
Author(s):  
Chonticha Saisawang ◽  
Jantana Wongsantichon ◽  
Albert J. Ketterman
Keyword(s):  
Drosophila Melanogaster ◽  
Cell Line ◽  
Glutathione Transferase ◽  
Embryonic Cell ◽  
Kinetic Properties ◽  
Genome Database ◽  
Reverse Transcription Pcr ◽  
Unique Character ◽  
Cytosolic Glutathione ◽  
Processed Pseudogene

The cytosolic GST (glutathione transferase) superfamily has been annotated in the Drosophila melanogaster genome database. Of 36 genes, four undergo alternative splicing to yield a total of 41 GST proteins. In the present study, we have obtained the 41 transcripts encoding proteins by RT (reverse transcription)–PCR using RNA template from Drosophila S2 cells, an embryonic cell line. This observation suggests that all of the annotated DmGSTs (D. melanogaster GSTs) in the proteome are expressed in the late embryonic stages of D. melanogaster. To avoid confusion in naming these numerous DmGSTs, we have designated them following the universal GST nomenclature as well as previous designations that fit within this classification. Furthermore, in the cell line, we identified an apparent processed pseudogene, gste8, in addition to two isoforms from the Delta class that have been published previously. Only approximately one-third of the expressed DmGSTs could be purified by conventional GSH affinity chromatography. The diverse kinetic properties as well as physiological substrate specificity of the DmGSTs are such that each individual enzyme displayed a unique character even compared with members from the same class.

scholarly journals Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site

2015 ◽  
Vol 35 (6) ◽  
Author(s):  
Jantana Wongsantichon ◽  
Robert C. Robinson ◽  
Albert J. Ketterman
Keyword(s):  
Drosophila Melanogaster ◽  
Active Site ◽  
Active Sites ◽  
Glutathione Transferase ◽  
Glutathione Transferases ◽  
Conserved Motif ◽  
Subunit Interface ◽  
Dimeric Subunit

Analysis of a new structure of an Epsilon class glutathione transferase from Drosophila melanogaster reveals a highly conserved motif that spans the dimeric subunit interface and connects the two active sites.

The importance of glutathione and glutathione transferase for somatic mutations in Drosophila melanogaster induced in vivo by 1,2-dichloroethane

1990 ◽  
Vol 11 (8) ◽  
pp. 1399-1402 ◽  
Author(s):  
Lennart Romert ◽  
Jan Magnusson ◽  
Claes Ramel
Keyword(s):  
Drosophila Melanogaster ◽  
Somatic Mutations ◽  
Glutathione Transferase

Author response for "Location and arrangement of campaniform sensilla in Drosophila melanogaster"

2020 ◽  
Author(s):  
Gesa F. Dinges ◽  
Alexander S. Chockley ◽  
Till Bockemühl ◽  
Kei Ito ◽  
Alexander Blanke ◽  
...  
Keyword(s):  
Drosophila Melanogaster ◽  
Author Response ◽  
Campaniform Sensilla

Live Confocal Analysis of Fertilization and Early Development

2001 ◽  
Vol 7 (S2) ◽  
pp. 1012-1013
Author(s):  
Uyen Tram ◽  
William Sullivan
Keyword(s):  
Drosophila Melanogaster ◽  
Embryonic Development ◽  
Real Time ◽  
Early Development ◽  
Fluorescent Probes ◽  
Primary Defect ◽  
Fluorescent Analysis ◽  
Dynamic Event ◽  
Enormous Amount ◽  
Fluorescent Studies

Embryonic development is a dynamic event and is best studied in live animals in real time. Much of our knowledge of the early events of embryogenesis, however, comes from immunofluourescent analysis of fixed embryos. While these studies provide an enormous amount of information about the organization of different structures during development, they can give only a static glimpse of a very dynamic event. More recently real-time fluorescent studies of living embryos have become much more routine and have given new insights to how different structures and organelles (chromosomes, centrosomes, cytoskeleton, etc.) are coordinately regulated. This is in large part due to the development of commercially available fluorescent probes, GFP technology, and newly developed sensitive fluorescent microscopes. For example, live confocal fluorescent analysis proved essential in determining the primary defect in mutations that disrupt early nuclear divisions in Drosophila melanogaster. For organisms in which GPF transgenics is not available, fluorescent probes that label DNA, microtubules, and actin are available for microinjection.

Apoptosis and development

2003 ◽  
Vol 39 ◽  
pp. 11-24 ◽  
Author(s):  
Justin V McCarthy
Keyword(s):  
Drosophila Melanogaster ◽  
Mammalian Cells ◽  
Cell Number ◽  
Model Organisms ◽  
Biological Processes ◽  
Nematode Caenorhabditis Elegans ◽  
Apoptotic Pathway ◽  
Genetic Pathways ◽  
Evolutionarily Conserved ◽  
Multicellular Organisms

Apoptosis is an evolutionarily conserved process used by multicellular organisms to developmentally regulate cell number or to eliminate cells that are potentially detrimental to the organism. The large diversity of regulators of apoptosis in mammalian cells and their numerous interactions complicate the analysis of their individual functions, particularly in development. The remarkable conservation of apoptotic mechanisms across species has allowed the genetic pathways of apoptosis determined in lower species, such as the nematode Caenorhabditis elegans and the fruitfly Drosophila melanogaster, to act as models for understanding the biology of apoptosis in mammalian cells. Though many components of the apoptotic pathway are conserved between species, the use of additional model organisms has revealed several important differences and supports the use of model organisms in deciphering complex biological processes such as apoptosis.

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