5'-Nucleotidase reverses the inhibitory action of actin on pancreatic deoxyribonuclease I.
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Biomedical subjects
Publications and source records attributed to G Rohr.
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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.
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A novel iodoacetamide label 4-perfluoro-tert-butyl-phenyliodoacetamide (PFP) containing nine fluorine atoms in equivalent positions has been synthesized. It provides a homogeneous 19F NMR resonance line which can be detected with high sensitivity when coupled to proteins. As an example, the sulfhydryl groups of actin have been labeled with PFP; < 100 nmol of this medium sized protein (corresponding to 2.5 mL of a 40 microM solution) can be detected easily in a single scan at 470 MHz.