Isolation and characterization of secretory actin . DNAase I complex from rat pancreatic juice.
DNAase I isolated from rat pancreatic juice was always found in association with a protein of molecular weight 43 000. This association leads to inhibition of the isolated rat pancreatic DNAase I activity by 66%. The molecular weight of the complex was found to be 74 000 by gel filtration indicating a 1 : 1 molar association of both proteins. Since the protein of molecular weight 43 000 has a number of properties similar to skeletal muscle actin such as filament formation, nucleotide binding, inhibition of the rat pancreatic DNAase I activity and comigration with skeletal muscle actin on polyacrylamide gels in the presence of dodecylsulfate, it is concluded that DNAase I is bound to actin in rat pancreatic juice in a 1 : 1 complex. It is demonstrated that a protein fraction from bile is able to activate the DNAase I enzymatic activity of the rat secretory actin . DNAase I complex.
D000199:Actins / Q000302:isolation & purification / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003851:Deoxyribonucleases / Q000302:isolation & purification / Q000378:metabolism; D008297:Male; D008854:Microscopy, Electron; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification; D010189:Pancreatic Juice / Q000201:enzymology*; D051381:Rats
D000199:Actins; D000596:Amino Acids; D009097:Multienzyme Complexes; D003851:Deoxyribonucleases