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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
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author Northrop, John H.
author_facet Northrop, John H.
author_sort Northrop, John H.
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description 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.
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spelling pubmed-21954012008-04-23 The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins Northrop, John H. J Gen Physiol Article 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. The Rockefeller University Press 1964-09-01 /pmc/articles/PMC2195401/ /pubmed/14212151 Text en Copyright © 1965 by The Rockefeller Institute Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Northrop, John H.
The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins
title The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins
title_full The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins
title_fullStr The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins
title_full_unstemmed The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins
title_short The Effect of Proteolytic Enzymes on E. coli Phages and on Native Proteins
title_sort effect of proteolytic enzymes on e. coli phages and on native proteins
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195401/
https://www.ncbi.nlm.nih.gov/pubmed/14212151
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