A HISTONE-LIKE FRACTION BOUND TO LIPID IN STAPHYLOCOCCUS EPIDERMIDIS
- 31 May 1965
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 43 (6) , 625-633
- https://doi.org/10.1139/o65-074
Abstract
The protein moiety of a proteolipid extracted from Staphylococcus epidermidis has been isolated. It was found to be highly basic, with lysine accounting for 25% of its amino acids. In vitro experiments showed that it readily formed a complex with DNA or RNA. The possible role of this protein fraction in cell stability and the Gram staining reaction is discusssed.This publication has 19 references indexed in Scilit:
- Deoxyribonucleoprotein of halophilic AchromobacterBiochimica et Biophysica Acta, 1962
- STUDIES ON THE COMPOSITION OF THE PROTEIN FROM ESCHERICHIA COLI RIBOSOMESProceedings of the National Academy of Sciences, 1961
- The Absence of Histone in the Bacterium Escherichia coli The Journal of cell biology, 1959
- Studies on nucleoproteins VI. The deoxyribonucleoprotein and the deoxyribonucleic acid of bovine tubercle bacilli (BCG)Biochimica et Biophysica Acta, 1958
- The chemical composition of the protoplast membrane of Micrococcus lysodeikticusBiochimica et Biophysica Acta, 1958
- Abnormal Properties of Histones from Malignant CellsNature, 1954
- Infrared Spectra and the Structure of Glycine and Leucine Peptides1Journal of the American Chemical Society, 1952
- Infrared Spectra of Some Proteins and Related SubstancesJournal of the American Chemical Society, 1949
- Nature of the Gram-positive Complex in Micro-organismsNature, 1945
- Histochemistry of the Gram-staining Reaction for Micro-organismsNature, 1943