Résumé
Background: Cutaneous calcifications or calcinosis cutis is an interesting lesion, wherein the skin, soft tissues and in the walls of small/medium sized veins, arteries. The aim of the present study is to evaluate the calcinosis cutis or cutaneous calcification prevalence and also its correlation with age, sex, site of the lesion, clinical features and histopathological findings. Methods: A 5 years prospective study was on 40 patients suspected to have calcinosis cutis. Surgical excision of skin lesions was also performed to do the histopathological study. Results: Women presented with lesions around the waist commonly. Males presented with lesions at different sites like over dorsum of legs and fore arm most commonly. Out of 40 cutaneous calcifications, 14 (35%) were Asymptomatic, 12 (30%) were painless papules/nodules, 8 (20%) were ulceration with or without discharge, 6 (15%) were painful papules/nodules. Conclusion: As the Cutaneous calcifications were mostly asymptomatic or painless, need to evaluate the carefully and treat if there is any underlying pathologies. Calcinosis cutis individuals should be educate and counsel regarding underlying pathologies and treatment.
Résumé
Background: The hard palate is an essential part of human skull, the detailed knowledge of which plays an important role in the passive articulation of speech. Methods: The present study was conducted on 65 dry skulls from the department of anatomy, MVJMC & RH, Bangalore. With vernier caliper, palatine length, palatine breadth and heights were measured. Palatine index and palatine height index were calculated. Results: Mean palatine length was 48.47 ± 4.66 mm. Mean palatine breadth was 36 ± 4.41 mm and height was 8.62 ± 2.76 mm. According to the palatine index range, 66% of the hard palate belongs to leptostaphyline, 18.5% belongs to mesostaphyline and 15. 5% was brachystaphyline. As per palatine height index, 72.3% of hard palate showed chamestaphyline followed by 26.1% orthostaphyline and 1.6% hypistaphyline. Conclusions: These observations can be utilised for ethnic and racial classification of crania, anthropological studies, fabricating complete maxillary dentures for edentulous patients and performing certain surgical procedures in hard palate & soft palate.
Résumé
Cibacron Blue F3G-A, a probe used to monitor nucleotide binding domains in enzymes, inhibited sheep liver 5, 10-methylenetetrahydrofolate reductase competitively with respect to 5-methyltetrahydrofolate and NADPH. The Ki values obtained by kinetic methods and the Kd value for the binding of the dye to the enzyme estimated by protein fluorescence quenching were in the range 0·9-1·2 μM. Another triazine dye, Procion Red HE-3B interacted with the enzyme in an essentially similar manner to that observed with Cibacron Blue F3G-A. These results as well as the interaction of the dye with the enzyme monitored by difference spectroscopy and intrinsic protein fluorescence quenching methods indicated that the dye was probably interacting at the active site of the enzyme by binding at a hydrophobic region.
Résumé
5,10-Methylenetetrahydrofolate reductase (EC 1.1.1.68) was purified from the cytosolic fraction of sheep liver by (NH4)2 SO4 fractionation, acid precipitation, DEAE-Sephacel chromatography and Blue Sepharose affinity chromatography. The homogeneity of the enzyme was established by sodium dodecyl sulphatepolyacrylamide gel electrophoresis, ultracentrifugation and Ouchterlony immunodiffusion test. The enzyme was a dimer of molecular weight 1,66,000 ± 5,000 with a subunit molecular weight of 87,000 ±5,000. The enzyme showed hyperbolic saturation pattern with 5-methyltetrahydrofolate. K0.5 values for 5-methyltetrahydrofolate menadione and NADPH were determined to be 132 μΜ, 2.45 μΜ and 16 μΜ. The parallel set of lines in the Lineweaver-Burk plot, when either NADPH or menadione was varied at different fixed concentrations of the other substrate; non-competitive inhibition, when NADPH was varied at different fixed concentrations of NADP; competitive inhibition, when menadione was varied at different fixed concentrations of NADP and the absence of inhibition by NADP at saturating concentration of menadione, clearly established that the kinetic mechanism of the reaction catalyzed by this enzyme was ping-pong.