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- Arnebrant, Thomas, et al.
(författare)
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Protein-surfactant interactions at solid surfaces
- 1995
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Ingår i: Proteins at Interfaces II Fundamentals and Applications. - Washington, DC : American Chemical Society. - 9780841233041 - 9780841215276 ; 602, s. 239-255
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Bokkapitel (refereegranskat)abstract
- Effects of surfactants on protein adsorption are reviewed. Differences between removal of preadsorbed proteins (elutability) and competitive adsorption are discussed and simple models are suggested. It can be concluded that surfactants may interact through solubilization or replacement mechanisms depending on surfactant- surface interactions and surfactant- protein binding. Solubilization requires complex formation between protein and surfactant, and the replacement adsorption of the surfactant to the surface. As for protein adsorption, one of the most important properties affecting the elutability appears to be the conformational stability. Differences between a competitive situation and addition of surfactant after adsorption of the protein are suggested to originate from alteration in surface activity of protein-surfactant complexes formed in solution as compared to pure protein, the difference in diffusivity of surfactants and protein, and time dependent conformational changes of the protein.
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- Larsson, Gerry, et al.
(författare)
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The Grossarth-Maticek and Eysenck personality types, health-related behaviour, and indicators of transitory ill-health
- 1995
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Ingår i: European Journal of Personality. - : SAGE Publications. - 0890-2070 .- 1099-0984. ; 9:2, s. 75-87
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Tidskriftsartikel (refereegranskat)abstract
- The aim of this study was to scrutinize the relationship between personality type as described by Grossarth-Maticek and Eysenck, health-related behaviours, and indicators of transitory ill health in a community sample. The sample consisted of all per sons aged 40 years (45 men and 35 women) in a Swedish municipality who agreed to take part in a health examination at the primary health care centre of the municipality. The Short Interpersonal Reactions Inventory (Grossarth-Maticek and Eysenck, 1990) was used to measure personality type. Self-report data were obtained regarding seven health-related behaviours. Health was assessed in three ways; self-report (paper and pencil), self-report (interview response to physician), and measures of 36 biological variables including immune system indicators. The allocation of persons to the different personality types proved problematic using the established methods. By combining the types, according to Eysenck's personality model, and performing a cluster analysis on this combination, a ‘healthy’ and a ‘stressed’ profile were identified within both the male and the female group of subjects. Persons in the healthy personality cluster showed more favourable scores on the health-related behaviour indices and on the self-report health scales than the persons in the stressed cluster. They also tended to score lower than those in the stressed cluster on most of the biological markers known to increase during acute stress. The possibility that this implies a higher level of strain for the persons in the stressed cluster on various bodily systems is discussed.
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- McGuire, J, et al.
(författare)
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Comparative Adsorption Studies with Synthetic, Structural Stability and Charge Mutants of Bacteriophage T4 Lysozyme.
- 1995
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Ingår i: Proteins at Interfaces II. - Washington, DC : American Chemical Society. - 9780841233041 - 9780841215276 ; 602, s. 52-65
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Bokkapitel (refereegranskat)abstract
- We have purified wild type, three structural stability mutants and four charge mutants of bacteriophage T4 lysozyme from E. coli strains harboring desired expression vectors. Structural stability mutants were produced by substitution of the isoleucine at amino acid position three, yielding a set of proteins with stabilities ranging from 1.2 kcal/mol greater, to 2.8 kcal/mol less, than that of the wild type. Charge mutants were produced by replacement of positively charged lysine residues with glutamic acid, yielding a set of molecules with formal charges ranging from +5 to +9 units. Adsorption kinetic data, along with the dodecyltrimethylammonium bromide-mediated elutability of each protein, has been monitored with in situ ellipsometry at hydrophobic and hydrophilic silica surfaces. A simple mechanism that allows adsorbing protein to adopt one of two states, each associated with a different resistance to elution and a different interfacial area occupied per molecule, has been used to assist interpretation of the adsorption data. Conditions implicit in the model have been used to estimate the fraction of molecules present on the surface just prior to surfactant addition that had adopted the more resistant state, and this fraction has been observed to correlate positively with resistance to elution. For the stability mutants, these properties were clearly related to protein stability as well. Concerning the charge mutants, results have not been clearly explainable in terms of protein net charge, but rather in terms of the probable influence of the location of each substitution relative to other mobile, solvent-exposed, charged side chains of the molecule.
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