Enzymatic properties of an extracellular phospholipase C purified from a marine streptomycete.
A novel extracellular phospholipase C (PLC) was purified from a marine streptomycete. It had a molecular mass of 28 kDa as estimated by SDS-polyacrylamide gel electrophoresis. Its enzyme activity was optimal at pH 8.0 at 45 degrees Celsius. The PLC hydrolyzed only phosphatidylcholine. Its activity was enhanced 300% by Na(+) (200 mM), suggesting that the purified PLC is a typical marine-type enzyme.
Mo
SangJoon
S
Department of Chemistry and Nano Science, Ewha Womans University, Seoul 120-750, Korea.
Kim
Jae-Heon
JH
Cho
Ki Woong
KW
D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D005110:Extracellular Space / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008386:Marine Biology; D013302:Streptomyces / Q000201:enzymology*; D010738:Type C Phospholipases / Q000302:isolation & purification / Q000378:metabolism*
D010738:Type C Phospholipases