Biomedical subjects
E Dickinson
Publications and source records attributed to E Dickinson.
Postmarketing surveillance studies.
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Time-dependent polymerization of beta-lactoglobulin through disulphide bonds at the oil-water interface in emulsions.
Time-dependent intermolecular sulphydryl-disulphide interchange involving beta-lactoglobulin adsorbed at the oil-water interface in n-tetradecane-in-water emulsions (10 wt% oil, 0.5 wt% protein, pH 7.0) has been investigated using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). While only monomers are detected in the adsorbed protein immediately after emulsion formation with pure beta-lactoglobulin, on storing the emulsion the amount of polymerized beta-lactoglobulin and the sizes of the oligomers are found to increase with time. There is no polymerization of adsorbed protein in emulsions made with pure alpha-lactalbumin after 72 h, or in emulsions made with beta-lactoglobulin in the presence of a reagent (N-ethylmaleimide) for modifying sulphydryl groups. Analysis by two-dimensional SDS-PAGE of adsorbed protein from aged emulsions made with a mixture of alpha-lactalbumin + beta-lactoglobulin shows some linking by disulphide bonds between alpha-lactalbumin and beta-lactoglobulin at the interface. Taken together with earlier time-dependent surface viscosity measurements, the results indicate the important role of free sulphydryl groups in the development of the high surface viscoelasticity of adsorbed globular proteins at the oil-water interface.
Surface shear viscometry as a probe of protein-protein interactions in mixed milk protein films adsorbed at the oil-water interface.
Time-dependent surface viscosities are reported for films adsorbed from binary mixtures of the proteins alpha-lactalbumin, beta-lactoglobulin and beta-casein. The measurements were made at a planar interface between n-tetradecane and various protein solutions (10(-3) wt% of each protein, pH 7, 25 degrees C) using a Couette-type torsion-wire surface viscometer operating at very low shear-rate. Differences in behaviour between simultaneous and sequential exposure of the pairs of proteins to the interface were investigated. Some experiments were performed with chemically modified beta-lactoglobulin samples whose disulphide bonds had been cleaved and blocked. Displacement of one protein by another (e.g. alpha-lactalbumin by beta-casein) is indicated by a sudden drop in surface viscosity immediately after addition of the second protein. In systems containing beta-lactoglobulin, the long-time surface viscosity is very sensitive to the adsorption time of beta-lactoglobulin prior to addition of the second protein. Blocking the disulphide bonds in beta-lactoglobulin leads to a much faster approach to a steady-state surface viscosity. This is interpreted in terms of a much more rapid unfolding of the disordered molecules of modified beta-lactoglobulin at the oil-water interface. We conclude that surface viscosity experiments give useful and sensitive information about competitive adsorption and cooperative interactions in mixed protein films.
The epidemiology of HIV transmission among paid plasma donors, Mexico City, Mexico.
Screening of blood product donations for antibody to HIV began in Mexico in May 1986. From June to October 1986, the HIV cumulative seroprevalence increased from 6.3 to 9.2% in a commercial plasma collection center. Of the 281 people who donated the antibody-positive units, 62 (22.1%) had documented seroconversion during these 5 months. An epidemiologic study of 54 seropositive and 58 seronegative donors was carried out. The HIV serologic status did not change in any of these donors after repeat testing. Only 13.0% of the seropositives and 15.5% of the seronegatives had any of the known risk factors for AIDS. There was a direct relationship between frequency of plasma donation and the risk of being seropositive. A survey of employees disclosed the frequent re-use of disposable blood collection equipment. We conclude that HIV transmission had probably occurred in this plasma collection center.
A sensitive analytical method for pyrrolizidine alkaloids. The mass spectra of retronecine derivatives.
The pyrrolizidine alkaloids in Senecio jacobaea can be hydrolyzed to the common base, retronecine, and derivatized to form the bistrifluoroacetate, bisheptafluorobutyrate, diacetate and bistrimethylsilyl ether. The analysis of the fluorinated compounds by electron capture provides sensitivity for detection of these alkaloids. The bond weakening effect in the ion formed on electron impact, between the allylic carbon and alkyl ester oxygen due to the electron withdrawing fluorinated groups of the ester, changes the driving force for fragmentation from the nitrogen alpha-cleavage reaction to a charge site migration. This yields alkyl-oxygen bond cleavage and formation of a stabilized allylic cation which is the base peak.
[The Mexican experience with personnel training in applied epidemiology].
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