The presence of two heat-stable inhibitors of phosphoprotein phosphatases in the dimorphic fungus, Mucor rouxii.
Two heat-stable inhibitors (a and b) of phosphoprotein phosphatases I and II from Mucor rouxii were isolated from mycelium of the fungus. They were partially purified from extracts by heating, DEAE-cellulose chromatography, and Sephadex G-75 gel filtration. The molecular weights of inhibitors a and b, estimated by gel filtration, are 5,000 and 20,000 respectively. Inhibitor a acts similarly on both enzymes while inhibitor b is relatively more active on enzyme II. Storage of inhibitor b at -20 degrees C for several weeks resulted in a partial conversion to a lower-molecular-weight form with properties similar to those of inhibitor a.
Seigelchifer
M A
MA
Passeron
S
S
D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D006358:Hot Temperature; D008970:Molecular Weight; D009089:Mucor / Q000032:analysis* / Q000201:enzymology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors*
D010749:Phosphoprotein Phosphatases