Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is known to interact with different biomolecules and was implicated in many novel cellular activities including programmed cell death, nuclear RNA transport unrelated to the commonly known carbohydrate metabolism. We reported here the purification of GAPDH from Chironomidae larvae (Insecta, Diptera) that showed different biologic activity towards heavy metals. It was inhibited by copper, cobalt nickel, iron and lead but was activated by zinc. The GAPDH was purified by ammonium sulphate fractionation and Chelating Sepharose CL-6B chromatography followed by Blue Sepharose CL-6B chromatography. The 150-kDa tetrameric GAPDH showed optimal activity at pH 8.5 and 37 °C. The multiple alignment of sequence of the Chironomidae GAPDH with other known species showed 78 - 88 % identity to the conserved regions of the GADPH. Bioinformatic analysis unveils substantial N-terminal sequence similarity of GAPDH of Chironomidae larvae to mammalian GADPHs. However, the GADPH of Chironomidae larvae showed different biologic activities and cytotoxicity towards heavy metals. The GAPDH enzyme would undergo adaptive molecular changes through binding at the active site leading to higher tolerance to heavy metals.
Keywords: Chironomidae, Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH), heavy metal, Zinc, copper.
Protein & Peptide Letters
Title:Glyceraldehyde-3-phosphate Dehydrogenase from Chironomidae Showed Differential Activity Towards Metals
Volume: 20 Issue: 9
Author(s): Isaac K.W. Chong and Wing S. Ho
Affiliation:
Keywords: Chironomidae, Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH), heavy metal, Zinc, copper.
Abstract: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is known to interact with different biomolecules and was implicated in many novel cellular activities including programmed cell death, nuclear RNA transport unrelated to the commonly known carbohydrate metabolism. We reported here the purification of GAPDH from Chironomidae larvae (Insecta, Diptera) that showed different biologic activity towards heavy metals. It was inhibited by copper, cobalt nickel, iron and lead but was activated by zinc. The GAPDH was purified by ammonium sulphate fractionation and Chelating Sepharose CL-6B chromatography followed by Blue Sepharose CL-6B chromatography. The 150-kDa tetrameric GAPDH showed optimal activity at pH 8.5 and 37 °C. The multiple alignment of sequence of the Chironomidae GAPDH with other known species showed 78 - 88 % identity to the conserved regions of the GADPH. Bioinformatic analysis unveils substantial N-terminal sequence similarity of GAPDH of Chironomidae larvae to mammalian GADPHs. However, the GADPH of Chironomidae larvae showed different biologic activities and cytotoxicity towards heavy metals. The GAPDH enzyme would undergo adaptive molecular changes through binding at the active site leading to higher tolerance to heavy metals.
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Cite this article as:
Chong K.W. Isaac and Ho S. Wing, Glyceraldehyde-3-phosphate Dehydrogenase from Chironomidae Showed Differential Activity Towards Metals, Protein & Peptide Letters 2013; 20 (9) . https://dx.doi.org/10.2174/0929866511320090002
DOI https://dx.doi.org/10.2174/0929866511320090002 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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