This project focused on the study of self-assembling systems that can be inuenced by an external magnetic field, following the PhD research of Hauke Carstensen. My role was to study the behavior of beads and to optimize the tunable parameters so that the main force driving the dynamics of the system is the magnetic dipolar interaction between beads. To make sure that no other force plays an important role, we checked a number of things, the most problematic of which is flocculation in the colloid, which may happen if some beads get stuck to each other; to prevent them from aggregating we have to make sure that they have a large zeta potential, which will result in an electrically repulsive force between beads and will thus increase the stability of the colloid. We also have to make sure that other forces in the sample do not exceed the magnitude of magnetic forces between particles; examples of such forces can be the drag experienced while moving in the viscous ferrofluid, the gravity force or the random thermal movement of the molecules in the fluid. In order to study these efects, I measured the zeta potential of the magnetic and non-magnetic beads and later I added a surfactant compound (SDS) to our sample in order to increase said potential.

<p>There is convincing research which shows that the enzyme alkaline phosphatase (ALP) has a central role in the mineralization of bone, more precisely that its catalytic activity is needed in the process. ALP is found on the surface of matrix vesicles where the mineral is formed. One theory about the function of the enzyme is that it binds to fibrous collagen in the bone and thereby incorporating the mineral into the bone. The purpose of this study is to establish whether ALP binds to collagen. If this is the case, more elaborate studies around this will be performed. The strength of the binding between collagen and the different types of ALP will be evaluated, as well as on which part of the collagen the binding occurs. The binding is going to be studied by constructing a method for the ÄKTApurifier system.</p><p> </p><p>Initially, the pureness of the different type of collagens was determined by using SDS-PAGE and the activity of the different types of ALP was established. These were also compared with a native PAGE. In SDS-PAGE, bovine type I collagen showed markings for a triple helix, a double helix and two single strains, α₁ and α₂. Bovine type II collagen showed markings for a double helix and α₁-strains. Human type I collagen showed markings for a triple helix, two double helixes, two α-strains and contaminations. Trials with collagen in Native PAGE did not provide any results. However, the trials with ALP revealed that the different types of ALP had different charge.</p><p> </p><p>Thereafter, blotting was performed. The results showed that all the different types of ALP, besides from E. coli, binds to bovine collagen type I and II and human collagen type I, however within various periods of time. In the trials with collagen coated plates the acquired results showed that some of the different types of ALP bind to collagen. ALP from liver binds the strongest to both collagen type I from rat and type IV from mouse. Intestinal ALP also binds to both types of collagen but not nearly as strong as liver ALP. Serum from rats did bind to collagen type I from rat but not to collagen type IV from mouse. ALP from kidney and human serum did not bind to either types of collagen. The trials concerning the ÄKTApurifier system were executed with ALP from liver alone because it had been proven to bind to bovine type I collagen through the previous methods. The results confirmed that ALP from liver binds to this type of collagen.</p><p> </p><p>The conclusions from this study are that ALP does indeed bind to collagen and does so to the triple helix and double helix form as well as the single strains of collagen. In other words the part of the structure in collagen that ALP binds to must exist in all three stages of collagen formation. Furthermore, it seems like some of the different types of ALP has a higher affinity for binding to collagen, as the time for binding to collagen varies for the different types of ALP. The results differed between methods concerning different types of ALP. Although, the method we consider to give the best result was blotting. However, the method using ÄKTApurifier can be complementary but needs further development.</p>

<p>Fotosyntesen kallas den process som omvandlar ljusenergi till kemisk energi. Fotosyntesen sker i tylakoidmembranet och drivs av två stora proteinkomplex, fotosystem II (PSII) och fotosystem I (PSI) då de tillförs energi i form av fotoner. PSI-N är ett mindre protein på ca 10 kDa som ingår i PSI. På något sätt, som ännu inte är klarlagt, samverkar PSI-N med PSI-F och plastocyanin när det dockar till PSI. Det är därför av viktigt att rena fram större mängder av PSI-N för att få djupare kunskaper om proteinet samt dess struktur och funktioner. Tidigare undersökningar har utförts i ämnet och ett fusionsprotein innehållande PSI-N har uttryckts i <em>Escherichia coli</em> (<em>E.coli</em>). Problem har dock uppstått efter lysis av cellerna då det har visat sig att fusionsproteinet har degraderats. Vårt examensarbete strävar efter att rena fram intakt fusionsprotein med hjälp av, framför allt, mekanisk lysis och proteasinhibitorer.</p> / <p>The process where light is converted into chemical energy is called photosyntesis. The reaction takes place in the thylakoid membrane and is driven by two major protein complexes, photosystem II (PSII) and photosystem I (PSI) when energy in form of photons are received. PSI-N, a subunit in PSI, is a smaller protein with a mass of approximately 10 kDa. In some way, which is not yet clarified, PSI-N collaborates with PSI-F and plastocyanin when plastocyanin is docking to PSI. It is therefore important to purify larger amounts of the protein to acquire deeper knowledge of its structure and function. In earlier research the PSI-N protein has been expressed in <em>Escherichia coli</em> (<em>E.coli</em>). The problem has been degradation of the fusion protein after lysis. Our goal with this project is to obtain the purified protein intact using mechanic lysis and protease inhibitors.</p>

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Studiens syfte är att genom en kvantitativ innehållsanalys ge svar på vilka artikeltyper och nyhetssammanhang som oftast förekommer för judendom, kristendom och islam – de tre abrahamitiska religionerna – i tidningarna Svenska Dagbladet (SvD) och Sydsvenskan (SDS) för perioderna april 2002, oktober 2002 och motsvarande för 2012. För att nå ökad förståelse för resultatet av den kvantitativa innehållsanalysen har intervjuer genomförts med en ledarskribent från vardera tidning samt med en representant från vardera religion. De intervjuade har bland annat fått ge sin uppfattning kring hur religionsnyheter ser ut idag jämfört med tio år sedan. Den kvantitativa studien består av 283 analyserade artiklar, av vilka 118 behandlar islam, 109 kristendom och 56 judendom. Kristendom dominerar för inrikesnyheterna och islam för utrikesnyheterna. Inom de inrikesartiklar som berör islam dominerar sammanhanget diskriminering, medan kultur och antisemitism utmärkte kristendom respektive judendom. För samtliga religioner är de dominerande sammanhangen för utrikesartiklarna annat och krig eller konflikt. I båda kategorier dominerar islam. De största skillnaderna åren emellan är antalet artiklar om Israel-Palestina-konflikten samt förekomsten av artiklar som rör antisemitism. Analyserat utifrån tidigare forskning och nyhetsvärderingsteorier tyder resultatet på att religiösa händelser är svåra att göra nyheter av, varför religionerna, och då särskilt islam och judendom, ofta förekommer i konfliktcentrerade nyheter – något även många av de intervjuade håller med om.

There is convincing research which shows that the enzyme alkaline phosphatase (ALP) has a central role in the mineralization of bone, more precisely that its catalytic activity is needed in the process. ALP is found on the surface of matrix vesicles where the mineral is formed. One theory about the function of the enzyme is that it binds to fibrous collagen in the bone and thereby incorporating the mineral into the bone. The purpose of this study is to establish whether ALP binds to collagen. If this is the case, more elaborate studies around this will be performed. The strength of the binding between collagen and the different types of ALP will be evaluated, as well as on which part of the collagen the binding occurs. The binding is going to be studied by constructing a method for the ÄKTApurifier system.   Initially, the pureness of the different type of collagens was determined by using SDS-PAGE and the activity of the different types of ALP was established. These were also compared with a native PAGE. In SDS-PAGE, bovine type I collagen showed markings for a triple helix, a double helix and two single strains, α1 and α2. Bovine type II collagen showed markings for a double helix and α1-strains. Human type I collagen showed markings for a triple helix, two double helixes, two α-strains and contaminations. Trials with collagen in Native PAGE did not provide any results. However, the trials with ALP revealed that the different types of ALP had different charge.   Thereafter, blotting was performed. The results showed that all the different types of ALP, besides from E. coli, binds to bovine collagen type I and II and human collagen type I, however within various periods of time. In the trials with collagen coated plates the acquired results showed that some of the different types of ALP bind to collagen. ALP from liver binds the strongest to both collagen type I from rat and type IV from mouse. Intestinal ALP also binds to both types of collagen but not nearly as strong as liver ALP. Serum from rats did bind to collagen type I from rat but not to collagen type IV from mouse. ALP from kidney and human serum did not bind to either types of collagen. The trials concerning the ÄKTApurifier system were executed with ALP from liver alone because it had been proven to bind to bovine type I collagen through the previous methods. The results confirmed that ALP from liver binds to this type of collagen.   The conclusions from this study are that ALP does indeed bind to collagen and does so to the triple helix and double helix form as well as the single strains of collagen. In other words the part of the structure in collagen that ALP binds to must exist in all three stages of collagen formation. Furthermore, it seems like some of the different types of ALP has a higher affinity for binding to collagen, as the time for binding to collagen varies for the different types of ALP. The results differed between methods concerning different types of ALP. Although, the method we consider to give the best result was blotting. However, the method using ÄKTApurifier can be complementary but needs further development.

Polymeric nanoparticles are potential candidates as carriers for pharmaceutical agents. Development of such nanoparticles generally requires molecules immobilized on the particle surfaces to ensure biocompatibility and/or targeting abilities. Following particle preparation and surface modification, excess reagents must be removed. Ultracentrifugation, which is the most widely used purification technique as per today, is not feasible in industrial applications. In this diploma work, tangential flow filtration is studied as an alternative purification method which is better suited for implementation in a large-scale process. Comparison of ultracentrifugation and tangential flow filtration in diafiltration mode for purification of nanoparticles, indicate that they are comparable with respect to particle stability and the removal of the surfactant SDS from methacrylic anhydride nanoparticles. The purification efficiency of tangential flow filtration is superior to that of ultracentrifugation. Conductivity measurements of filtrates and supernatant liquids show that a stable conductivity value can be reached 6 times faster in filtration than in centrifugation with equipment and settings used. This conductivity arises from several types of molecules, and the contribution from surfactant molecules alone is not known. However, protein adsorption on the particles indicates successful removal of surfactant. Conductivity and tensiometry were evaluated as potential methods to quantify surfactant in solutions, but both proved unsatisfactory. Using bovine serum albumin as a model protein, the extent of immobilization to nanoparticles is evaluated at different pH. A maximum amount of 6,8 mg/m2 is immobilized, whereof an unknown part is covalently bound. This coverage is achieved at pH 4,0 and is probably partly due to low electrostatic repulsion between particle and protein. An estimation of 2,0 µmol covalently bound BSA per gram of nanoparticles corresponds to 5,3 mg/m2 and a surface coverage of 76%. Removal of excess reagents after surface modification is done with ultracentrifugation instead of filtration, as particle aggregates present after the immobilization reaction might foul the membrane.

In this study, a new bacteriocin isolated from a Leuconostoc mesenteroides subsp. cremoris strain was purified to homogeneity by pH mediated cell adsorption-desorption, solid phase extraction with Amberlite XAD-16, cation-exchange chromatography and hydrophobic interaction chromatography. The purification resulted in an electrophoretically pure protein that was smaller than 6 kDa as judged by SDS-PAGE. The bacteriocin was found to be very hydrophobic and cationic and could be adsorbed by synthetic calcium silicate due to its cationic and especially hydrophobic nature. It was observed that this bacteriocin was sensitive to &amp / #945 / -amylase in addition to proteinase K, trypsine, pepsine and chymotrypsine and had a bactericidal mode of action with a concomitant cell lysis. The results indicated that bacteriocin produced by Leuconostoc mesenteroides subsp. cremoris was more stable to combined effect of pH and heat than nisin, lacticin 481, lacticin 3147 and lactococcin G and was bactericidal between pH 2.0-12. It was found that the bacteriocin produced by Leuconostoc mesenteroides subsp. cremoris was stable to organic solvents and could be extracted with chloroform containing solvents efficiently for purification. The bacteriocin produced by Leuconostoc mesenteroides subsp. cremoris was found to have a strong inhibitory activity against Listeria innoqua, Listeria monocytogenes, Bacillus cereus, Enterococcus faecalis, Lactobacillus delbrueckii, Lactobacillus cremoris, other Leuconostoc meenteroides strains and gram-negative bacterium Pseudomonas fluorescens. Some of the insensitive bacteria were observed to be sensitive when high concentration of the bacteriocin was used.

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<p>The aim of this thesis work was to investigate theadsorption of surfactants to different nonpolar interfaces.Particularly, the effects of the polar group and the nature ofthe hydrophobic interface were elucidated. The interfacialbehavior of the liquid-vapor interface was investigated bymeans of surface tension measurements. Here the effect of thepolar group and the hydrocarbon chain length was investigatedin a systematic manner. It was found that the shorter of thetwo chains examined, decyl, generated a larger surface pressurecontribution than the longer, dodecyl. Furthermore, the sugarbased surfactants behaved differently as compared to theethylene oxide based ones. The former could be modelled byassuming a hard disc behavior of the head group while thelatter displayed polymeric behavior. The influence of saltconcentration on the surface tension behavior of an ionicsurfactant, sodium dodecyl sulphate, was investigated. Theresult could be rationalized by employing the Gouy- Chapmanmodel to the polar region. Furthermore, mixtures of two sugarbased surfactants were investigated by surface tensionmeasurements and the adsorbed amount of the two components atthe interface atdifferent concentrations and fractions in thebulk were obtained by applying the Gibbs surface tensionequation. It was found that the molecule with the smaller headgroup adsorbed preferentially, and more so as the totalsurfactant concentration was increased. These findings could beexplained by considering the interactions generated by thedifferent head groups. The adsorption of sugar surfactants toan isolated hydrophobic surface was studied by means of wettingmeasurements and the behavior was similar to that at theliquid-vapor interface. Wetting isotherms were measured on twodifferent hydrophobic surfaces where the covalently attachedhydrophobic layers were in a crystalline and fluid state,respectively. The wetting results revealed that the sugarsurfactants anchored in the fluid hydrophobic layer. This had asignificant influence on the force profile. For example, at thecrystalline surface the surfactant monolayers were easilyremoved as the surface came into contact at relatively lowapplied loads. This was not the case when the hydrophobic layerwas in a fluid state. Here a significant fraction of thesurfactants remained between the surfaces. Disjoining pressureisotherms were measured using a sugar based surfactant thatwere thoroughly purified and compared to the as receivedsample. Even the purified sample showed a double-layer forcealthough lower as compared to the as received, one. Asignificant difference in foam stability was also observed.</p>