GALP

(redirected from Glyceraldehyde 3-phosphate)
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AcronymDefinition
GALPGlyceraldehyde 3-phosphate
GALPGood Automated Laboratory Practices
GALPGames, Argumentation, and Logic Programming (symposium)
References in periodicals archive ?
XBP1, X-box binding protein 1; usXBP1, un-spliced XBP1; sXBP1, spliced XBP1; RT-PCR, Reverse transcription polymerase chain reaction; qPCR, quantitative real-time polymerase chain reaction; ANOVA, analysis of variance; HSD, honestly significant difference; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.
ELISA: enzyme-linked immunosorbent assay; GAPDH: glyceraldehyde 3-phosphate dehydrogenase; qRT-PCR: quantitative reverse transcription polymerase chain reaction; TNF-[alpha]: tumor necrosis factor-alpha.
Table 3 shows the results of the docking study between compounds 1-12 with the enzyme glyceraldehyde 3-phosphate dehydrogenase.
Expression was determined relative to glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and then each expression level was compared to the level of the normal control group.
(ANOVA followed by Bonferroni's test.) BZYQD: Bu-Zhong-Yi-Qi decoction; LC3: microtubule-associated protein light chain-3; GAPDH: glyceraldehyde 3-phosphate dehydrogenase; 3-MA: 3-methyladenine.
DAPI, 4,'6-diamidino-2- phenylindole; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; FITC, fluorescein isothiocyanate; TUNEL, terminal deoxynucleotidyl transferase dUTP nick-end labeling.
The list of primers for specific genes and housekeeping gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) are indicated in Table 2.
Fructose-1, 6-bisphosphate aldolase is an essential glycolytic enzyme found in Saccharomyces cerevisiae, which catalyzes the cleavage of fructose 1, 6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (3).
Human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was amplified as a control for the polymerase chain reaction (PCR).
The primers for T7RNAP, EGFP and Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were as following:
Most of the enzymes involved in different metabolic pathways such as plastidic aldolases (ALD, spot 12, 2.69-fold, and spot 36, 1.5-fold), fructose bisphosphatase aldolase class I (FBA, spot 36, 1.5-fold), glyceraldehyde 3-phosphate dehydrogenase (GAPDH, spot 6, 1.8 fold, spot 23, 3.1 fold, and spot 37,1.6 fold), Ribose-5-phosphate,3-epimerase (spot 41, 1.7 fold), triose-phosphateisomerase (spot 42, 1.6 fold and spot 44, 1.9-fold), and carbonic anhydrase (CA, spot 17, 3.1 fold, spot 27, 3.22 fold, and spot 40, 1.64-fold) were increased in relative abundance in 100 [micro]M As treatment except for transketolase (TK; spot 1) and RuBisCO activase (spot 22).