TY  - BOOK
AU  - Shanmugan Balabhaskaran
AU  - Muniandy Sekaran
TI  - Purification and properties of glutathione S-transferase from latex of Hevea brasiliensis
PY  - 1993///
PB  - Journal of Natural Rubber Research
KW  - Glutathione s-transferase
KW  - Hevea brasiliensis
N2  - Glutathione S-transferase was purified more than 500-fold with a recovery of 50;from the latex of Hevea brasiliensis. The purification steps involved affinity chromatography, ion-exchange chromatography and gel filtration. The moecular weight of the native enzyme was 50 000 Daltons as determined by gel filtration while sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed the presence of one type of sub-unit with a molecular weight of 23 000 daltons. Substrate specificity studies revealed the enzyme to have limited specificity. The N-terminal amino acid was determined to be glycine while the isoelectric point of this enzyme was estimated to be 4.3. The enzyme exhibited multiplicity on ion-exchange chromatography which could be abolished if the column was eluted with thiol reagents
ER  -