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The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins

Lambda coli phage is not inactivated by chymotrypsin, trypsin, or ficin. T(2) phage is slowly inactivated by high concentrations of (α-, β-, γ-, or Δ-chymotrypsin, but not by trypsin or ficin. P(1) phage is slowly inactivated by α-, β-, or γ-chymotrypsin, or ficin, more rapidly by Δ-chymotrypsin, an...

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Detalles Bibliográficos
Autor principal: Northrop, John H.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1964
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195401/
https://www.ncbi.nlm.nih.gov/pubmed/14212151
Descripción
Sumario:Lambda coli phage is not inactivated by chymotrypsin, trypsin, or ficin. T(2) phage is slowly inactivated by high concentrations of (α-, β-, γ-, or Δ-chymotrypsin, but not by trypsin or ficin. P(1) phage is slowly inactivated by α-, β-, or γ-chymotrypsin, or ficin, more rapidly by Δ-chymotrypsin, and much more rapidly by trypsin. Crystalline egg albumin, crystalline serum albumin, E. coli nucleoprotein, and yeast nucleoprotein are hydrolyzed slowly by α-chymotrypsin. Yeast nucleoprotein, like P(1) phage, is hydrolyzed more rapidly by Δ-chymotrypsin than by α-chymotrypsin, but not by trypsin or ficin. Neither phages nor native proteins were attacked by papain, carboxypeptidase, deoxyribonuclease, or ribonuclease.