scholarly journals Polynucleotide Phosphorylase of Micrococcus luteus (Micrococcus lysodeikticus)

1968 ◽  
Vol 243 (19) ◽  
pp. 5094-5100 ◽  
Author(s):  
C B Klee ◽  
M F Singer
Keyword(s):  
Micrococcus Luteus ◽  
Polynucleotide Phosphorylase ◽  
Micrococcus Lysodeikticus

scholarly journals The effect of trypsin digestion on the activities of polynucleotide phosphorylase

1967 ◽  
Vol 105 (1) ◽  
pp. 25-33 ◽  
Author(s):  
P. S. Fitt ◽  
E. A. Fitt
Keyword(s):  
Nucleic Acids ◽  
Differential Effect ◽  
Gel Filtration ◽  
Trypsin Digestion ◽  
Uridine Diphosphate ◽  
Polynucleotide Phosphorylase ◽  
Polycytidylic Acid ◽  
Micrococcus Lysodeikticus ◽  
Preferential Loss ◽  
Cytidine Diphosphate

1. Treatment of Micrococcus lysodeikticus polynucleotide phosphorylase (nucleoside diphosphate–polynucleotide nucleotidyltransferase) with trypsin causes a preferential loss of its cytidine diphosphate and uridine diphosphate polymerization activities. 2. The phosphorolytic activity of the enzyme towards polycytidylic acid is unaffected in conditions in which the cytidine diphosphate-polymerization activity without added primer is virtually abolished. 3. The treated enzyme retains its altered pattern of activities when purified fivefold by gel filtration. 4. The effect on the cytidine diphosphate-polymerization activity is due, in part, to a large increase in primer requirement as a result of proteolysis, and is qualitatively independent of the state of purity of the polynucleotide phosphorylase. 5. The enzyme is protected from trypsin degradation by nucleic acids, polynucleotides and nucleoside disphosphates. 6. A similar, but less marked differential effect, is caused by α-chymotrypsin.

scholarly journals Polynucleotide Phosphorylase of Micrococcus lysodeikticus

1964 ◽  
Vol 239 (3) ◽  
pp. 893-901
Author(s):  
Faith N. Brenneman ◽  
Maxine F. Singer
Keyword(s):  
Polynucleotide Phosphorylase ◽  
Micrococcus Lysodeikticus
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