Isolation from lugworm (Arenicola cristata) of four proteases that activate cyclic AMP phosphodiesterase.
1. Four cyclic AMP phosphodiesterase-activating activities, designated as A, B, C and D, were isolated from lugworm, Arenicola cristata, by preparative flat-bed isoelectric focusing. Activators C and D were further purified by TSK 3000SW HPLC to homogeneity. 2. Activators A, B, C, and D corresponded to pIs of 4.4, 5.0, 5.2 and 5.4; their mol wts were estimated to be 36,200, 30,500, 30,200 and 28,300 respectively. 3. The protease nature of these activities were confirmed by the inhibition by several trypsin inhibitors of their activation of phosphodiesterase and by their hydrolysis of TAME, a synthetic trypsin substrate. Only protease A also hydrolyzed BTEE, a chymotrypsin substrate.
Parker
G R
GR
Department of Chemistry, Tennessee State University, Nashville 37203.
Lin
Y M
YM
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology; D002147:Calmodulin / Q000302:isolation & purification / Q000378:metabolism; D004789:Enzyme Activation; D007700:Kinetics; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D011077:Polychaeta / Q000201:enzymology*; D013552:Swine
D002147:Calmodulin; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D010447:Peptide Hydrolases