Skip to main content
The Journal of General Physiology logoLink to The Journal of General Physiology
. 1964 Sep 1;48(1):73–78. doi: 10.1085/jgp.48.1.73

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

John H Northrop 1
PMCID: PMC2195401  PMID: 14212151

Abstract

Lambda coli phage is not inactivated by chymotrypsin, trypsin, or ficin. T2 phage is slowly inactivated by high concentrations of (α-, β-, γ-, or Δ-chymotrypsin, but not by trypsin or ficin. P1 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 P1 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.

Full Text

The Full Text of this article is available as a PDF (317.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anson M. L. CRYSTALLINE CARBOXYPOLYPEPTIDASE. Science. 1935 May 10;81(2106):467–468. doi: 10.1126/science.81.2106.467. [DOI] [PubMed] [Google Scholar]
  2. BERTANI G. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol. 1951 Sep;62(3):293–300. doi: 10.1128/jb.62.3.293-300.1951. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CHENG P. Y. The inactivation of group B arthropod-borne animal viruses by proteases. Virology. 1958 Aug;6(1):129–136. doi: 10.1016/0042-6822(58)90064-3. [DOI] [PubMed] [Google Scholar]
  4. Lederberg E M, Lederberg J. Genetic Studies of Lysogenicity in Escherichia Coli. Genetics. 1953 Jan;38(1):51–64. doi: 10.1093/genetics/38.1.51. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Northrop J. H., Technical Assistance of Marie King THE EFFECT OF TRYPSIN, CHYMOTRYPSIN, RIBONUCLEASE, AND DESOXYRIBONUCLEASE ON ACTIVE, INACTIVE, AND REVERSIBLY INACTIVATED MEGATHERIUM PHAGE. J Gen Physiol. 1955 Nov 20;39(2):251–258. doi: 10.1085/jgp.39.2.251. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from The Journal of General Physiology are provided here courtesy of The Rockefeller University Press

RESOURCES