Examination of Surface Adsorption of Cetyltrimethylammonium Bromide and Sodium Dodecyl Sulfate

2011 ◽  
Vol 115 (29) ◽  
pp. 9077-9086 ◽  
Author(s):  
Hiromichi Nakahara ◽  
Osamu Shibata ◽  
Yoshikiyo Moroi
2013 ◽  
Vol 29 (02) ◽  
pp. 351-357 ◽  
Author(s):  
FAN Hai-Ming ◽  
◽  
◽  
ZHANG Yi-Nuo ◽  
ZHANG Jin ◽  
...  

2003 ◽  
Vol 49 (12) ◽  
pp. 775-779 ◽  
Author(s):  
Soumitra Rajagopal ◽  
Nicole Eis ◽  
Kenneth W Nickerson

In liquid culture, eight typical Gram-negative bacteria were ca. 10 000-fold more sensitive to cationic detergents than to the anionic detergent sodium dodecyl sulfate. Cetyltrimethylammonium bromide (CTAB) was inhibitory at concentrations ranging from 0.0006% to 0.01%. Four pseudomonads able to form biofilms were ca. 1000-fold more resistant to CTAB on Luria–Bertani agar plates than they were in liquid culture. A lasI mutant of Pseudomonas aerugi nosa was only able to tolerate 0.1% CTAB on Luria–Bertani agar plates but could tolerate 5% CTAB when supplemented with homoserine lactone containing culture supernatants.Key words: sodium dodecyl sulfate, cetyltrimethylammonium bromide, bacterial detergent resistance, homoserine lactones, Pseudomonas biofilms.


1980 ◽  
Vol 43 (02) ◽  
pp. 124-126 ◽  
Author(s):  
Christine Mannhalter ◽  
Sandra Schiffman

SummaryThese experiments study surface adsorption of native and activated factor XI using purified radiolabelled human factor XI and trypsin activated factor XI. Both forms of factor XI adsorb not only to glass but also to polypropylene, polyethylene and polystyrene. Albumin (10 mg/ml) markedly reduces adsorption to plastics but not to glass. Sodium dodecyl sulfate prevents adsorption to all surfaces tested. Reduction of 125I-activated factor XI in the presence of sodium dodecyl sulfate yields labelled chains of molecular weight of about 46,000 (heavy chain), 37,000 (light chain) and a further breakdown product of about 26,000. Reduction of activated factor XI in glass or plastic in the absence of sodium dodecyl sulfate yields only light chain and breakdown product in solution; heavy chain is removed by adsorption. Therefore, we conclude that the adsorption site (s) in trypsin activated factor XI and presumably also in native factor XI is (are) located in the heavy chain subunit of the molecule.


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