Citation
Subramaniam P., . and Balabaskaran S., . and Kumar Das V.G., . (1993) Purification of the basic form of glutathione s-transferase from Achatina fulica snail. [Proceedings Paper]
Abstract
The glutathione S-tranferase EC 2.5.1.18GST are multifunctional enzymes which are also involved in detoxication of xenobiotics. They catalyse the conjugation of glutathione GSH to various electrophiles. In this study the cationic form of GST was purified from the snail Achatina fulica using ion-exchange and affinity chromatography to apparent homogenity. Native PAGE confirmed the homogenity of the protein purified. From SDS-PAGE the molecular weight of the protein was 53 200 daltons. In immunoelectrophoresis experiments a single preciptin arc was observed towards the cathode. Amino acid analysis of the purified protein was also conducted
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Abstract
The glutathione S-tranferase EC 2.5.1.18GST are multifunctional enzymes which are also involved in detoxication of xenobiotics. They catalyse the conjugation of glutathione GSH to various electrophiles. In this study the cationic form of GST was purified from the snail Achatina fulica using ion-exchange and affinity chromatography to apparent homogenity. Native PAGE confirmed the homogenity of the protein purified. From SDS-PAGE the molecular weight of the protein was 53 200 daltons. In immunoelectrophoresis experiments a single preciptin arc was observed towards the cathode. Amino acid analysis of the purified protein was also conducted
Additional Metadata
| Item Type: | Proceedings Paper |
|---|---|
| Additional Information: | Summaries En Ms |
| AGROVOC Term: | ACHATINA FULICA |
| AGROVOC Term: | PURIFICACION |
| AGROVOC Term: | CROMATOGRAFIA |
| AGROVOC Term: | TRANSFERASAS |
| AGROVOC Term: | INMUNOELECTROFORESIS |
| Geographical Term: | MALAYSIA |
| Depositing User: | Ms. Norfaezah Khomsan |
| Last Modified: | 24 Apr 2025 05:26 |
| URI: | http://webagris.upm.edu.my/id/eprint/15432 |
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