Isolation and Purification of Endotoxin by Hydrolytic Enzymes
Overview
Affiliations
Various commercial hydrolases were used in an attempt to degrade the endotoxic lipopolysaccharide macromolecule. Some inert components, such as peptides and nucleic acids, could be removed from endotoxin preparations. As a result, endotoxic activity, measured by pyrogenicity, Shwartzman reaction, and mouse lethality, was increased. The remarkable resistance of endotoxin to hydrolases led to the use of such enzymes for the liberation and purification of endotoxin from whole bacterial cells.
Komazin G, Maybin M, Woodard R, Scior T, Schwudke D, Schombel U J Biol Chem. 2019; 294(50):19405-19423.
PMID: 31704704 PMC: 6916509. DOI: 10.1074/jbc.RA119.010836.
Release of toxic microvesicles by Actinobacillus actinomycetemcomitans.
Nowotny A, Behling U, Hammond B, Lai C, Listgarten M, Pham P Infect Immun. 1982; 37(1):151-4.
PMID: 7049947 PMC: 347503. DOI: 10.1128/iai.37.1.151-154.1982.
Investigations on the specificity of the Limulus test for the detection of endotoxin.
Wildfeuer A, HEYMER B, Schleifer K, HAFERKAMP O Appl Microbiol. 1974; 28(5):867-71.
PMID: 4613271 PMC: 186840. DOI: 10.1128/am.28.5.867-871.1974.
Wildfeuer A, HEYMER B, Schleifer K, Seidel H, HAFERKAMP O Klin Wochenschr. 1974; 52(4):175-8.
PMID: 4601042 DOI: 10.1007/BF01614393.
Kreutzer D, ROBERTSON D Infect Immun. 1979; 23(3):819-28.
PMID: 110683 PMC: 414238. DOI: 10.1128/iai.23.3.819-828.1979.