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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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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1964
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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. |
collection | PubMed |
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. |
format | Text |
id | pubmed-2195401 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1964 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
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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