THE EFFECTS OF MAMMALIAN AND OTHER CATIONIC POLYPEPTIDES ON THE CYTOCHEMICAL CHARACTER OF BACTERIAL CELLS
Open Access
- 1 December 1961
- journal article
- research article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 114 (6) , 1063-1078
- https://doi.org/10.1084/jem.114.6.1063
Abstract
Cationic polypeptides interact with bacterial cells of E. coli and B. anthracis. They confer upon the cells some of the characteristics of cationic particles. Since bacterial cells usually behave as anions, acidic dyes at high pH levels differentiate between cells which have and those which have not interacted with cationic polypeptides. Under the conditions of these experiments it appeared that cationic polypeptides tend to be sorbed in highest concentration in the surface layers of the cells. Electrovalent binding to anionic cell components and detergent action are probably among the mechanisms involved in the interaction between the polypeptides such as histones and bacterial cells.Keywords
This publication has 13 references indexed in Scilit:
- [Activity of various histones isolated from calf thymus on Escherichia coli and Mycobacteria].1959
- BACTERICIDAL ACTION OF HISTONEThe Journal of Experimental Medicine, 1958
- THE EFFECT OF SALMINE ON BACTERIACanadian Journal of Microbiology, 1958
- COMPARATIVE STUDIES ON CHROMATOGRAPHICALLY PURIFIED HISTONESJournal of Biological Chemistry, 1957
- Characterization of an Antibacterial Peptide from Calf Thymus.Experimental Biology and Medicine, 1956
- [An effect of proteins on bacteria which is dependent upon isoelectric point].1954
- The Absorption of Polymyxin E by Bacteria and Bacterial Cell Walls and its Bactericidal ActionJournal of General Microbiology, 1953
- A Selective Staining Method for the Basic Proteins of Cell NucleiProceedings of the National Academy of Sciences, 1953
- The agglutination and growth inhibition of bacteria by lysine polypeptidesArchives of Biochemistry and Biophysics, 1952
- Antibacterial Properties of Protamine and HistoneScience, 1942