Open AccessIsolation and Characterization of Secretory Actin · DNAase I Complex from Rat Pancreatic Juice
Author(s) -
ROHR Gerhard,
MANNHERZ Hans Georg
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb20907.x
Subject(s) - chemistry , size exclusion chromatography , actin , biochemistry , pancreatic juice , skeletal muscle , microbiology and biotechnology , enzyme , biology , pancreas , endocrinology
DNAase I isolated from rat pancreatic juice was always found in association with a protein of molecular weight 43000. 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 74000 by gel filtration indicating a 1 : 1 molar association of both proteins. Since the protein of molecular weight 43000 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.