Purification of microbial asparaginases by the aid of affinity chromatography
1975
: Asparaginases from Escherichia coli and Erwinia caratovora were isolated and purified by column chromatography with a specific sorbent (sepharose, covalently bound to N-alpha-(6-aminohexyl)-D-asparagine). Homogenous asparaginase from E. coli was isolated by one-step procedure, while the enzyme from Er. carotovara was 50-60-fold purified. Asparaginase from Mycobacterium n. sp. was found not to bind with the specific sorbent.
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