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ARGININE-RICH PROTEINS OF POLYMORPHONUCLEAR LEUKOCYTE LYSOSOMES
- Source :
- The Journal of Experimental Medicine
- Publication Year :
- 1968
- Publisher :
- Rockefeller University Press, 1968.
-
Abstract
- The cationic antibacterial proteins of rabbit PMN lysosomes have been resolved into at least five subfractions. Each of these showed substantial selectivity in its antibacterial action against several pathogenic bacteria, including two smooth and two rough Escherichia coli strains, three Staphylococcus aureus strains, one S. albus, three proteus species and four different cultures of streptococcus. Each of the subfractions possesses a different electrophoretic mobility. Amino acid analyses of the three most cationic components revealed high contents of arginine consistent with their relative electrophoretic mobilities and very high arginine to lysine ratios. Aromatic amino acids were present in very low concentrations in these proteins and their light absorption at 2800 A was correspondingly weak. The evidence of antibacterial specificity, along with marked differences in the arginine-lysine ratios, shows that the cationic antibacterial components of rabbit PMN lysosomes are biologically and chemically heterogeneous.
- Subjects :
- Electrophoresis
Paper
Blood Bactericidal Activity
Sucrose
Arginine
Staphylococcus
Immunology
Lysine
Biology
medicine.disease_cause
Article
chemistry.chemical_compound
Escherichia coli
Leukocytes
medicine
Aromatic amino acids
Animals
Immunology and Allergy
chemistry.chemical_classification
Bacteria
Streptococcus
Pathogenic bacteria
Proteus
biology.organism_classification
Amino acid
chemistry
Biochemistry
Staphylococcus aureus
Rabbits
Lysosomes
Subjects
Details
- ISSN :
- 15409538 and 00221007
- Volume :
- 127
- Database :
- OpenAIRE
- Journal :
- Journal of Experimental Medicine
- Accession number :
- edsair.doi.dedup.....17e51294438dddde72cf7a0983de4ba8