Journal of Protein Chemistry 2003-05-01

An enzyme based dechlorination of a polychlorinated biphenyl (PCB) mixture, Aroclor 1248, using glutathione S-transferases from the northern quahog Mercenaria mercenaria.

Brian N Blanchette, Bal Ram Singh

Index: J. Protein Chem. 22(4) , 377-86, (2003)

Full Text: HTML

Abstract

The glutathione S-transferases from the northern quahog (Mercenaria mercenaria) from control and contaminated sites were subjected to incubation with polychlorinated biphenyls in an Aroclor 1248 mixture. Subsequent solvent-solvent extraction and gas chromatographic analysis revealed that 2 of the 28 congeners present in the Aroclor 1248 mixture were affected by the presence of the GST. The first of the aforementioned congeners with a retention time of 36.7 min by gas chromatographic analysis decreased in total content. The largest decrease in the 36.7 min peak was the result of incubation with GSTs purified from quahogs taken from the Superfund site in New Bedford Harbor, New Bedford, MA. The second of the affected congeners with a retention time of 59 min showed an increase, which could result from the glutathione conjugation to the PCB congener. The Aroclor 1248 mixture (a limited number of its constituent congeners) also acts as a competitive inhibitor of the GST activity, which is indicative of a substance interacting with the free GST in solution. The ultimate result of the conjugation of the PCB congener to GSH would be the formation of a hydrophillic conjugate of an otherwise insoluble PCB. The PCB-GSH conjugating activity of the quahog GSTs may ultimately serve as a tool for PCB remediation.