PURIFICATION OF HUMAN PLATELET MONOAMINE OXIDASE B BY HIGH PERFORMANCE LIQUID CHROMATOGRAPHY.

Ghulam Ansari, Nutan T. Patel, Richard R. Fritz, Creed W. Abell

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Abstract

Human platelet monoamine oxidase (MAO B), a membrane bound enzyme was purified to homogeneity by DEAE-Sephacel column chromatography, chromatofocusing, and high performance liquid chromatography (HPLC). The crucial purification step was HPLC on a anion exchange column (SynChropak AX 300). The HPLC column was eluted initially with potassium phosphate buffer (100 mM, pH 7. 4) for 10 min at a flow rate of 1. 0 ml/min, followed by a gradient (0-1%) of octyl- beta -D-glucopyranoside (octylglucoside) in the same buffer for 10 min, and finally with buffered octylglucoside (1%) for 40 min. The extent of homogeneity and the subunit M//r (approximately 59,000) of MAO B were determined by sodium-dodecyl sulfate polyacrylamide gel electrophoresis followed by silver staining for proteins.

Original languageEnglish (US)
Pages (from-to)1407-1419
Number of pages13
JournalJournal of Liquid Chromatography
Volume6
Issue number8
StatePublished - 1983

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ASJC Scopus subject areas

  • Molecular Medicine

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