Purification of nonantibiotic insulinase inhibitors from bacitracin.

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Medina V, Kesner L, Stracher A

Purification of nonantibiotic insulinase inhibitors from bacitracin.

Biochem Med Metab Biol. 1993 Apr;49(2):255-64.

PubMed ID

8484964 [ View in PubMed

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Abstract

Bacitracin is commonly used in metabolic studies as an insulinase inhibitor. The many isoforms of the commercial preparation were fractionated by charge and size in order to find the most active rat-muscle insulinase inhibitors. CM-Sepharose chromatography revealed that most of the inhibitory activity was contained in a fraction (CM-Inh) that amounted to less than 5% of the mixture. The CM-Inh fraction could be further separated by size on Bio-Gel P4 columns. Six subgroups, each with characteristic specific activity, were isolated. The most potent inhibitor fractions have no antibiotic activity and have molecular weights about twice that of bacitracin A. The peaks isolated by means of Bio-Gel P4 chromatography can be further fractionated by reversed phase HPLC on a C8 column, and by electrophoresis on nonreducing acrylamide gels.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Bacitracin	Insulin-degrading enzyme	Protein	Humans	Yes	Inhibitor	Details