Effect of NaF on type-1 phosphatase aggregation.
In muscle cytosolic and glycogen fractions prepared in the presence of 50 mM NaF phosphorylase phosphatase was a approximately 70 kDa complex instead of the 250 kDa or higher seen in the absence of NaF. A approximately 70 kDa complex was also formed when purified 37 kDa phosphatase-1 catalytic subunit (but not its 33 kDa tryptic fragment) was exposed to NaF. Treating this latter complex with a cross-linker led to disappearance of the 37 kDa protein and formation of a approximately 66 kDa band (detected by SDS electrophoresis), thus indicating the dimeric nature of the approximately 70 kDa complex.
Pesi
R
R
Ist. di Patologia Generale, Universita di Pisa, Italy.
Villa-Moruzzi
E
E
D000818:Animals; D002850:Chromatography, Gel; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors*; D010765:Phosphorylase Phosphatase / Q000037:antagonists & inhibitors*; D054645:Protein Phosphatase 1; D011817:Rabbits; D012969:Sodium Fluoride / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000494:pharmacology
D046911:Macromolecular Substances; D012969:Sodium Fluoride; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; D010765:Phosphorylase Phosphatase; D014357:Trypsin