Abstract
Hemoglobin, its chains, and myoglobin enhance the antibiotic activity of colicine K. These proteins also interact with colicine K and other O antigens to alter their serological activity. The hemoglobin proteins did not alter the serological activities of three Pneumococcus polysaccharides or T4 bacteriophage DNA antigens but did alter the antigenic activity of fetuin. Interaction of hemoglobin and colicine K resulted in a retardation of colicine K antibiotic moiety as measured by gel filtration but did not affect the gel filtration properties of the lipopolysaccharide moiety.
Keywords
ANTIBIOTICS
ANTIGENS
CHROMATOGRAPHY
COLICINS
COLIPHAGES
COMPLEMENT FIXATION TESTS
DIPLOCOCCUS PNEUMONIAE
EXPERIMENTAL LAB STUDY
FETUIN
GEL FILTRATION
HEMOGLOBIN
IONS
MYOGLOBIN
POLYSACCHARIDES
BACTERIAL
SERUM GLOBULINS
MeSH Terms
Anti-Bacterial Agents
Antigens
Chromatography
Chromatography, Gel
Colicins
Coliphages
Complement Fixation Tests
Endotoxins
Fetuins
Hemoglobins
Ions
Myoglobin
Polysaccharides
Polysaccharides, Bacterial
Research
Serum Globulins
Streptococcus pneumoniae
alpha-Fetoproteins
Chemicals
Anti-Bacterial Agents
Antigens
Colicins
Endotoxins
Fetuins
Hemoglobins
Ions
Myoglobin
Polysaccharides
Polysaccharides, Bacterial
Serum Globulins
alpha-Fetoproteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
VANVUNAKIS H
RUFFILLI A
LEVINE L
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17 references, click to expand
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