ABSTRACT
We report the case of a 73-year-old male who presented with a chronic subdural hematoma that compressed the frontal lobe, an area known to be active in detrusor control, and caused contralateral hemiparesis and urgency incontinence. Urodynamically, he had a small bladder capacity and high amplitude overactive detrusor contractions with an intact sphincteric response. We concluded that the effect of intracranial lesions on voiding depends upon the site rather than the type of the pathology. Further in-depth studies are needed to clarify the effect of intracranial lesions, and accordingly the function of different brain regions and their influence on voiding.
Subject(s)
Hematoma, Subdural, Chronic/complications , Urination Disorders/complications , Aged , Brain/pathology , Electromyography/methods , Fluoroscopy/methods , Humans , Male , Paresis , Tomography, X-Ray Computed/methods , Urinary Bladder/pathology , UrodynamicsABSTRACT
The objective of the current study was to formulate solid lipid nanoparticles of oxybenzone to enhance its sunscreening efficacy while reducing its side effects. Solid lipid nanoparticles (SLNs) of oxybenzone were prepared by the solvent diffusion method. A complete 2(4) factorial design was used to optimize preparations. The study design involves the investigation of four independent variables, namely lipid type (Glyceryl monostearate, GMS; and Witepsol E85, WE85), lipid concentration (5 and 10%), polyvinyl alcohol (PVA) concentration (1 and 2%), and ethanol/acetone ratios (1:1 and 3:1, v/v), in terms of their effect on the particle size and entrapment efficiency. GMS was found to significantly increase the p.s. and EE%. SLNs prepared using 10% lipid had slower drug release compared to those prepared using 5%. The candidate oxybenzone-loaded SLN formula (SLN2) consisting of 0.5% oxybenzone, 10% GMS, 1% PVA, and ethanol/acetone (1:1, v/v) was then formulated into a gel and compared to the corresponding free oxybenzone nanosuspension and placebo SLN. The formulations were evaluated for skin irritation, in vitro sun protection factor, and ultraviolet A protection factors. The incorporation of oxybenzone into solid lipid nanoparticles greatly increased the SPF and UVA protection factor of oxybenzone more than five-fold while providing the advantage of overcoming skin irritancy problems.
Subject(s)
Drug Carriers , Drug Compounding , Chemistry, Pharmaceutical , Lipids , Nanoparticles , Particle SizeABSTRACT
Sulfathiazole and povidone were coacervated by many methods, indicating complexation of the two compounds. The coacervated complex had a higher solubility and dissolution rate than did sulfathiazole. It resisted the action of dilute acids and alkalies, suggesting a helical structure with sulfathiazole situated between two povidone chains and a hydrogen bond linking the amino groups of the sulfathiazole to the oxygen of povidone. Upon addition of precipitants for sulfathiazole, the povidone portion attempted to compensate and to solubilize the whole complex; hence, partial precipitation or coacervation occurred. A model is given to describe the dissolution profile of the different coacervate systems prepared.
Subject(s)
Povidone , Sulfathiazoles , Chemical Precipitation , Drug Interactions , Ethanol , Resorcinols , Sodium Hydroxide , Solubility , Solvents , SulfathiazoleABSTRACT
Samples of bovine muscle were frozen at -5 degrees, -10 degrees, -20 degrees, -40 degrees, -60 degreese, -80 degreese, and -196 degrees C at slow (about 1 degrees/10 min) and high freezing rate (maximum 1 degrres/0.05 min) and subsequently thawed at room temerature. The changes in the extractable activity ("total activity") of the enzymes aconitase (AC), fumarase (FU) succine dehydrogenase (SDH), glutamic oxaloacetic transaminase (GOT), the mitochondrial isozyme of the COT (GOTM) and glutamate pyruvate transaminase (GPT) by freezing and thawing were studied. Neither the temperature nor the rate of freezing influenced the total activity of these enzymes. The subcellular distribution of these enzymes was investigated by determination of the enzyme activities in the muscle press juice. Freezing at -5 degrees C hat only little influence, but between -10 degrees and -40 degrees or -60 degrees C the release of AC, FU, GOTM and GPT from the mitochondria into the sarcoplasma increased with falling temperature, apparently by increasing damage of the mitochondria. The extent of this effect was not significantly influenced by the rat of freezing. Between -60 degrees and -196 degrees C no further rise of this effect was observed. A release of SDH did not occur at all conditions of freezing. It is suggested that the damage of muscle mitochondria by freezing and thawing is mainly due to a dehydration process.
