Purification and properties of glutathione S-transferases from larvae of Wiseana cervinata
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Purification and properties of glutathione S-transferases from larvae of Wiseana cervinata.
The glutathione S-transferases from the porina moth, Wiseanna cervinata, were purified by affinity chromatography, cation-exchange chromatography and preparative isoelectrofocusing. The major transferase (IV) was purified to homogeneity by a factor of 530-fold with a yield of 83%. Other transferases present were purified to a smaller degree (approx. 50-fold) to a stage of near-homogeneity. The ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1984
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2170041