onr:"swepub:oai:lup.lub.lu.se:e02a58f5-f7ea-41ed-b088-622b3b3fde92"
Search: onr:"swepub:oai:lup.lub.lu.se:e02a58f5-f7ea-41ed-b088-622b3b3fde92" > The Influence of Ne...
- 1 of 1
- Previous record
- Next record
- To hitlist
The Influence of Net Charge and Charge Location on Adsorption and Dodecyltrimethylammonium Bromide-Mediated Elutability of Bacteriophage T4 Lysozyme at Silica Surfaces
-
- McGuire, J (author)
- Lund University
-
- Wahlgren, M (author)
- Lund University,Lunds universitet,Avdelningen för livsmedel och läkemedel,Institutionen för processteknik och tillämpad biovetenskap,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Food and Pharma,Department of Process and Life Science Engineering,Departments at LTH,Faculty of Engineering, LTH
-
- Arnebrant, T (author)
- Lund University
- (creator_code:org_t)
- Elsevier BV, 1995
- 1995
- English 10 s.
- In: Journal of Colloid and Interface Science. - : Elsevier BV. - 1095-7103 .- 0021-9797. ; 170:1, s. 193-202
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- The effect of net charge and charge location on the adsorption and dodecyltrimethylammonium bromide (DTAB)-mediated elutability of bacteriophage T4 lysozyme was monitored at hydrophilic and hydrophobic silica surfaces with in situ ellipsometry. Mutant lysozymes were produced by substitution of selected lysine residues with glutamic acid, each substitution thus decreasing the net charge of the protein by 2 units. The wild-type protein (net charge +9) and four mutant proteins, each of net charge +7 or +5, were purified from Escherichia coli strains harboring the desired expression vectors. Differences in interfacial behavior among the proteins were observed with respect to both the adsorption kinetics and the DTAB-mediated elutability exhibited by each. No simple relationship between protein net charge and surface behavior was observed, indicating that the location of the charge replacements had the major effect on surface behavior. At hydrophilic surfaces, mutations allowing the most mobile regions of positive charge to more readily orient toward the interface increased that protein's resistance to elutability; at hydrophobic surfaces, mutations favoring or otherwise not inhibiting hydrophobic association between the protein and the surface increased the resistance to elutability. This was not related to protein net charge, but to the probable influence of the location of each substitution relative to the other mobile, solvent-exposed, charged side chains of the molecule.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Annan teknik -- Livsmedelsteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Other Engineering and Technologies -- Food Engineering (hsv//eng)
Publication and Content Type
- art (subject category)
- ref (subject category)
Find in a library
- Journal of Colloid and Interface Science (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- McGuire, J
- Wahlgren, M
- Arnebrant, T
- About the subject
-
- ENGINEERING AND TECHNOLOGY
- ENGINEERING AND ...
- and Other Engineerin ...
- and Food Engineering
- Articles in the publication
- Journal of Collo ...
- By the university
- Lund University
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
