A novel inositol-phospholipid-specific phospholipase C. Rapid purification and characterization.
A novel bovine brain inositol-phospholipid-specific phospholipase C has been identified on the basis of chromatographic behaviour and purified to apparent homogeneity by a rapid three-step procedure. The purified enzyme has a molecular mass of 85 kDa on SDS/polyacrylamide gel electrophoresis and a specific activity of 24 mumol.min-1.mg-1. The enzyme is dependent on Ca2+ and shows a marked preference for inositol phospholipid substrates. The unique nature of this polypeptide was confirmed through partial protein sequence analysis.
Meldrum
E
E
Ludwig Institute for Cancer Research, London, UK.
Katan
M
M
Parker
P
P
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000201:enzymology / Q000378:metabolism; D002417:Cattle; D002845:Chromatography / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007295:Inositol Phosphates / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010455:Peptides / Q000302:isolation & purification; D010743:Phospholipids / Q000378:metabolism*; D013403:Sugar Phosphates / Q000378:metabolism*; D010738:Type C Phospholipases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism
D007295:Inositol Phosphates; D010446:Peptide Fragments; D010455:Peptides; D010743:Phospholipids; D013403:Sugar Phosphates; D010738:Type C Phospholipases