A study by polyacrylamide-gel electrophoresis of the effect of proteolysis on Micrococcus lysodeikticus polynucleotide phosphorylase.
1. Trypsin digestion of Micrococcus lysodeikticus polynucleotide phosphorylase (nucleoside diphosphate-polynucleotide nucleotidyltransferase) causes a progressive increase in electrophoretic mobility in polyacrylamide gels of the single active degradation product. 2. A marked increase in primer requirement for CDP polymerization occurs before a more mobile product is formed. 3. alpha-Chymotrypsin digestion yields a product that separates into several active species on polyacrylamide-gel electrophoretograms. 4. No separation of ADP-and CDP-polymerization activities occurs during electrophoresis after either trypsin or alpha-chymotrypsin treatment.
D000227:Adenine Nucleotides; D002918:Chymotrypsin; D003597:Cytosine Nucleotides; D004586:Electrophoresis; D005782:Gels; D008837:Micrococcus / Q000201:enzymology*; D009713:Nucleotidyltransferases; D014357:Trypsin
D000227:Adenine Nucleotides; D003597:Cytosine Nucleotides; D005782:Gels; D009713:Nucleotidyltransferases; D002918:Chymotrypsin; D014357:Trypsin