[A survey of non-approved blood donors in Ume]. Every seventh donor was not rejected, low Hb level was the most common cause].
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Adult↗
Biomedical subjects
C G Axelsson
Publications and source records attributed to C G Axelsson.
[Let us avoid cholesterol tests performed by pharmacies!].
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Cholesterol↗
Changes in structure and hydrophobic surface properties of beta-lactoglobulin determined by partition in aqueous two-phase polymeric systems.
The non-polar surface properties of beta-lactoglobulin and especially its interaction with poly(ethylene glycol)-bound palmitate has been studied as a function of pH, temperature and protein concentration. The maximum interaction between beta-lactoglobulin and polymer-bound palmitate occurs at pH 4.3 and pH 7.8. The change in conformation of beta-lactoglobulin around pH 7.5 seems to involve exposure of apolar amino acids to the solvent which results in an increased affinity for hydrocarbons. This is contrary to the situation at pH 4.8--6.0 where the corresponding change in conformation does not affect the protein-hydrocarbon interaction. The results suggest that partition studies in an aqueous two-phase system is a very useful tool to detect changes in conformation and aggregation and to characterize the corresponding hydrophobic surface properties of a protein.
Animals↗
Histone-hydrocarbon interaction. Partition of histones in aqueous two-phase systems containing poly(ethylene glycol)-bound hydrocarbons.
The hydrophobic properties of histones have been examined with help of the two-phase partition technique using dextran-poly(ethylene glycol)-water systems. We have found that different fatty acid esters of poly(ethylene glycol) interact with total histones in a manner similar to proteins of the type beta-lactoglobulin and serum albumins. Thus the maximum interaction occurs when the fatty acid contains 16-18 carbon atoms. With less than eight carbon atoms in the polymer-bound fatty acid, no histone-hydrocarbon interaction is observed. The interaction of the five individual histone fractions with palmitate depends on the type of salt used and on its concentration. We suggest that the histones can be divided into three groups with decreasing hydrophobic properties: H3, H2a greater than H4, H2b greater than H1.
Histones↗
Hydrophobic interaction determined by partition in aqueous two-phase systems. Partition of proteins in systems containing fatty-acid esters of poly(ethylene glycol).
In this report we describe a new method which is useful for measuring hydrophobic interactions between aliphatic hydrocarbon chains and proteins in aqueous environment. The method is based on partition of proteins in an aqueous two-phase system containing dextran and poly(ethylene glycol) and different fatty acid esters of poly(ethylene glycol). The partition is measured under conditions where contributions from electrostatic interactions are eliminated. The difference in partition of proteins in phase systems with and without hyrocarbon groups bound to poly(ethylene glycol), deltalog K, where K is the partition coefficient, is taken as a measure of hydrophobic interaction. Deltalog K varies with size of hydrocarbon chain and type of protein. The length of the aliphatic chain should be greater than 8 carbon atoms in order to get a measurable effect in terms of deltalog K. Bovine serum albumin, beta-lactoglobulin, hemoglobin and myoglobin have been shown to have different affinities for palmitic acid ester of poly(ethylene glycol). No hydrophobic effect could be observed for ovalbumin, cytochrome c or alpha-chymotrypsinogen A.
Binding Sites↗