Unknown

Dataset Information

0

A study by polyacrylamide-gel electrophoresis of the effect of proteolysis on Micrococcus lysodeikticus polynucleotide phosphorylase.


ABSTRACT: 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.

SUBMITTER: Fitt PS 

PROVIDER: S-EPMC1187375 | biostudies-other | 1968 Dec

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1153513 | biostudies-other
| S-EPMC2834601 | biostudies-literature
| S-EPMC2860026 | biostudies-literature
| S-EPMC2795571 | biostudies-literature
| S-EPMC1161998 | biostudies-other
| S-EPMC6777840 | biostudies-literature
| S-EPMC3568550 | biostudies-literature
| S-EPMC6352729 | biostudies-literature
| S-EPMC5293606 | biostudies-literature
| S-EPMC1144099 | biostudies-other