منابع مشابه
Mechanisms of anionic detergent-induced hemolysis.
The effect of osmotic protectors (sucrose and polyethylene glycols) and of a decrease in the detergent concentration at different points of hemolysis of human erythrocytes by sodium dodecyl sulphate on the shape of kinetic curves of hemolysis were studied. It is shown that slow detergent-induced hemolysis follows the colloid-osmotic mechanisms. Evidence is provided that rapid hemolysis by sodiu...
متن کامل'Detergent-like' permeabilization of anionic lipid vesicles by melittin.
Melittin (MLT), the 26-residue toxic peptide from the European honeybee Apis mellifera, is widely used for studying the principles of membrane permeabilization by antimicrobial and other host-defense peptides. A striking property of MLT is that its ability to permeabilize zwitterionic phospholipid vesicles is dramatically reduced upon the addition of anionic lipids. Because the mechanism of per...
متن کاملIsolation of a strain of Pseudomonas putida capable of metabolizing anionic detergent sodium dodecyl sulfate (SDS)
BACKGROUND AND OBJECTIVES Sodium Dodecyl Sulfate (SDS) is one of the most widely used anionic detergents. The present study deals with isolation and identification of SDS-degrading bacteria from a detergent contaminated pond situated in Varanasi city, India. MATERIALS AND METHODS Employing enrichment technique in minimal medium (PBM), SDS-degrading bacteria were isolated from pond water sampl...
متن کاملImproving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis.
Cutinase is an enzyme suitable for detergent applications as well as for organic synthesis in non-aqueous solvents. However, its inactivation in the presence of anionic surfactants is a problem which we have addressed by creating a complete saturation library. For this, the cutinase gene from Fusarium solani pisi was mutated to incorporate all 19 possible amino acid exchanges at each of the 214...
متن کاملMultimeric forms of the small multidrug resistance protein EmrE in anionic detergent.
Escherichia coli multidrug resistance protein E (EmrE) is a four transmembrane alpha-helix protein, and a member of the small multidrug resistance protein family that confers resistance to a broad range of quaternary cation compounds (QCC) via proton motive force. The multimeric states of EmrE protein during transport or ligand binding are variable and specific to the conditions of study. To ex...
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ژورنال
عنوان ژورنال: Journal of Investigative Dermatology
سال: 1960
ISSN: 0022-202X
DOI: 10.1038/jid.1960.119