Dermatoscopic screening in family practice.

BACKGROUND: Screening for dermatologic lesions is important in primary care medicine and may be enhanced by magnified illuminated video images. Viewing skin lesions with a dermatoscopic instrument is very helpful in judging and evaluating their characteristics. Both patients and physicians benefit from the improved diagnostic yield, possible medical-legal protection, enhanced development of the patient-physician relationship, medical practice economic boost, and more efficient dermatologic screening. The higher magnification and illuminated view theoretically enables the physician to make better decisions and helps convince the patient to comply with recommended treatment. METHODS: 57 patients in a single private family practice were interviewed before receiving a visual dermatology screening examination. The physician then recorded his findings and suggested plan. Next, the physician performed a magnified video dermatologic examination and once again recorded his findings, plan, and impression of the patient's reaction to the recommendations and treatment. RESULTS: 57 patients with 79 examination sites demonstrated an increased confidence by both the physician and patient with the video examination over the traditional dermatologic examination. In addition, several changes in proposed treatment were noted following the video examination. CONCLUSIONS: Both the patients and physician believed the magnified video dermatologic examination improved diagnostic accuracy and increased patient motivation to act on physician recommendations.

Carbon-13 and proton nuclear magnetic resonance spectroscopy of water-soluble porphyrins and metalloporphyrins.

Carbon-13 and proton nuclear magnetic resonance (NMR) spectra have been recorded for porphyrins, zinc porphyrins, and iron(III) porphyrin complexes in aqueous media. Spectra of porphyrin-c and hemin-c confirm the structure with thioether linkages at positions alpha to the porphyrin ring. The pattern of NMR isotropic shifts has implications regarding electron transfer in cytochrome-c. Free-base porphyrin-c and meso-substituted porphyrins have been examined for pyrrole nitrogen-hydrogen tautomerism and possible aggregation in aqueous solution. Zinc porphyrin 13C NMR spectra were recorded in order to provide diamagnetic references for paramagnetic iron(III) derivatives. Low-spin iron(III) porphyrin-biscyano complexes in aqueous solution exhibit NMR isotropic shift patterns similar to those previously observed for related compounds in non-aqueous media. The first 13C NMR spectra are reported for mu-oxo-bridged iron(III) porphyrin dimers. A partially resolved spectrum of a high-spin iron(III) porphyrin has also been obtained. Patterns of 13C and proton isotropic shifts are compared, and unpaired spin delocalization mechanisms for 13C resonances are discussed in a qualitative manner.

A whole blood control for the Coulter Model S.

The white cell count, red cell count, haemoglobin, and mean cell volume of a new preserved whole blood preparations used as a control material for the Coulter Model S were found to be stable for at least two months. This material provides a cheap and stable whole blood control which is now in routine use in 18 laboratories throughout Wales.

Carbon-13 nuclear magnetic resonance of heme carbonyls. Cytochrome c and carboxymethyl derivatives of cytochrome c.

Carbonyl complexes of horse cytochrome c and various carboxymethylated derivatives have been examined using 13C NMR (carbon-13 nuclear magnetic resonance) spectroscopy. The multiplicity and chemical shift of the 13CO resonance were found to be functions of pH and the extent of alkylation. Correlations have been made among prominent features of the chemical shift titration curves and changes in the environment of the heme. A simple model compatible with the bulk of previous observations has been suggested to account for the several carbonyl resonance peaks and the complex behavior of the chemical shift with changes in pH.

Carbon-13 nuclear-magnetic-resonance spectroscopy of whole cells and of cytochrome C from Neurospora crass grown with (S-Me-13C)methionine.

Neurospora crassa cytochrome C biosynthetically labelled with [S-Me-13C]methionine was prepared and analysed by 13C nuclear-magnetic-resonance spectroscopy. The methyl group of methionine is extensively incorporated into an N-trimethyl-lysine-72 residue arise from S-adenosylmethionine transmethylation, and that the methyl carbons of methionine residues are sufficiently close to the haem centre to experience chemical shifts from the ring currents of the tetrapyrrole pi electrons and broadening due to binding of methionine-80 with the haem, as well as interaction of the S-E113C]methyl groups with the paramagnetic iron centre. Although whole cells of the labelled Neurospora produced a 13C resonance at the expected position for the methionyl methyl group most of the methyl label was diverted into N-tetra-alkyl ammonium compounds. After an active state of growth these labelled N-methyl compounds appear, in the main, to be low-molecular-weight derivatives of choline which, if associated with membrane, are in a sufficiently fluid environment to have short rotational correlation times. During a subsequent dormant growth period these compounds become associated to some extent with relatively more immobile phases as a result of membrane binding or an increase in membrane rigidity.

Carbon-13 nuclear magnetic resonance spectroscopy of [2-13C]carboxymethylcytochrome c.

Horse heart cytochrome c has been carboxymethylated under various reaction conditions using [2-13C]bromoacetate. Direct analysis of reaction products using 13C nuclear magnetic resonance spectroscopy shows that the protein can be much more extensively modified than has previously been assumed. The proximity of one carboxymethylmethionine residue to the paramagnetic center of the ferric protein allows it to be distinguished from a more constant carboxymethylmethionine residue on the basis of the chemical shift of its labeled methylene group. Refolding of cytochrome c after alkylation at low pH apparently gives a different configuration of modified methionine residues within the protein compared to that produced by alkylation at neutral pH in the presence of cyanide.