G1881
α-Glycerophosphate Dehydrogenase-Triosephosphate Isomerase from rabbit muscle
Type III, ammonium sulfate suspension
Synonyme(s) :
GDH/TIM, α-GDH-TPI
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A propos de cet article
Biological source:
rabbit muscle
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Laissez-nous vous aiderbiological source
rabbit muscle
type
Type III
form
ammonium sulfate suspension
GDH activity
75-200 units/mg protein (biuret)
TPI activity
750-2000 units/mg protein
storage temp.
2-8°C
Quality Level
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Catégories apparentées
General description
Research area: Neuroscience
α-Glycerophosphate Dehydrogenase-Triosephosphate isomerase (α-GDH-TPI or GDH/TIM) is an enzyme mixture of α-glycerophosphate dehydrogenase (GDH) and triosephosphate isomerase (TPI).
α-Glycerophosphate Dehydrogenase-Triosephosphate isomerase (α-GDH-TPI or GDH/TIM) is an enzyme mixture of α-glycerophosphate dehydrogenase (GDH) and triosephosphate isomerase (TPI).
Application
α-Glycerophosphate Dehydrogenase-Triosephosphate Isomerase from rabbit muscle has been used in spectrophotometric aldolase assay and fructose 2,6 bisphosphate assay. It has also been used in erythrocyte transketolase (ETK) activity to study the prevalence of and factors associated with thiamin deficiency in obese.
α-glycerophosphate dehydrogenase was used in 2-deoxy-ribose 5-phosphate aldolase (DERA) cleavage (retroaldol) assay.
Biochem/physiol Actions
α-Glycerophosphate dehydrogenase (α-GPDH) has the ability to produce reactive oxygen species (ROS), that is induced by Ca2+.
α-glycerophosphate dehydrogenase catalyzes the conversion of dihydroxyacetone to glycerol phosphate. α-Glycerophosphate dehydrogenase (α-GPDH) has the ability to produce reactive oxygen species (ROS), that is induced by Ca2+. Triosephosphate isomerase (TPI) is an essential enzyme in the glycolytic pathway, responsible for converting dihydroxyacetone phosphate (DHAP) into glyceraldehyde-3 phosphate (GAP). TPI′s role is crucial in enhancing the efficiency of the catabolic process within glycolysis. However, a deficiency in TPI can lead to glycolytic enzymopathies, rare genetic disorders characterized by neurologic dysfunction and hemolytic anemia.
Packaging
(Sold on the basis of α-GDH units.)
Physical form
Mixed crystalline suspension in 3.2 M (NH4)2SO4, with 0.05 g/L EDTA, pH 6.0
Other Notes
(α-GDH) One unit will convert 1.0 μmole of dihydroxyacetone phosphate to α-glycerophosphate per min at pH 7.4 at 25 °C.
(TPI) One unit will convert 1.0 μmole of D-glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 at 25 °C.
Classe de stockage
12 - Non Combustible Liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
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The role of mitochondrial dehydrogenases in the generation of oxidative stress
Adam-Vizi V and Tretter L
Neurochemistry International, 62(5), 757-763 (2013)
Structural and Genetic Studies Demonstrate Neurologic Dysfunction in Triosephosphate Isomerase Deficiency Is Associated with Impaired Synaptic Vesicle Dynamics
Roland BP, et al.
PLoS Genetics, 12(3) (2016)
D Roberts et al.
The Biochemical journal, 183(2), 349-360 (1979-11-01)
1. The fluorescent ATP analogue 1,N6-etheno-ATP is a good substrate and an efficient allosteric inhibitor of rabbit skeletal-muscle phosphofructokinase. 2. Fluorescence energy transfer occurs between bound 1,N6-etheno-ATP and phosphofructokinase. 1,N6-Etheno-ATP fluorescence is enhanced, intrinsic protein fluorescence is quenched, and the
C R Hussey et al.
European journal of biochemistry, 80(2), 497-506 (1977-11-01)
A preparation of phosphofructokinase from rabbit skeletal muscle is described which exploits the association-dissociation properties of the enzyme. Phosphofructokinase to prepared is partially phosphorylated and may be fractioned into three distinct species with sedimentation coefficients of 30 S, 18 S
Identification of an anaerobically induced phosphoenolpyruvate-dependent fructose-specific phosphotransferase system and evidence for the Embden-Meyerhof glycolytic pathway in the heterofermentative bacterium Lactobacillus brevis.
Saier M H, et al.
Journal of Bacteriology, 178(1) (1996)
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