Disorders of the distal radioulnar joint.

Disorders of the distal radioulnar joint can be classified into functional abnormalities based on instability, incongruity of the joint surface, impaction, and isolated triangular fibrocartilage complex tears. Knowledge of the type of lesion aids in selecting the treatment option best suited to correcting each problem. This review begins by summarizing the anatomy of the distal radioulnar joint. It then examines the various clinical problems that may arise in this complicated anatomic area and outlines the different surgical and nonsurgical options available to treat these disorders. The most important aspect in treatment of disorders of the distal radioulnar joint is early recognition, followed by prompt appropriate surgical or nonsurgical management.

Effects of several selected odorants on the sodium- and potassium-dependent adenosine triphosphatase activities of two different chicken olfactory tuberinals.

The NaK-adenosine triphosphatase (ATPase)-rich nerve-ending particle preparations (B fractions) of the epithelial tissue of chicken olfactory tubercle and the olfactory main concha were isolated by differential centrifugation. These tissues were exposed to the following odorants: 2-nonanone, 1-nonanol, 1-octanol, (+)2-octanol, and (-)2-octanol. There was a significant stimulation of NaK-ATPase by 2-nonanone (1 x 10(-3) M) in the B fraction of the olfactory tubercle and olfactory main concha. The NaK-ATPase increased significantly in the B fraction response of the olfactory main concha with 1 x 10(-3) M of 1-octanol but NaK-ATPase declined significantly in the presence of 1 x 10(-3) M of 1-nonanol. Both optical and structural isomers of odorants were shown to elicit different responses in NaK-ATPase activity. It is proposed that interactions between the odorant molecules and the membrane bound NaK-ATPase complex lead to recognition of odor by chickens.

A lente intraocular de camara anterior. Suas vantagens, requisitos e os fundamentos de um novo desenho. / Anterior chamber intraocular lens: advantages, requirements and basis of a new design

O autor propoe uma nova lente de camara anterior, de sua autoria.Relaciona uma serie de qualidades, extraidas de muitas outras ja em uso, as quais estariam reunidas nesta sua lente. Enumera uma serie de vantagens em defesa das lentes de camara anterior

Odorous chemical perturbations of (Na+ + K+)-dependent ATPase activities. Effects on native and lipid-substituted preparations from individual turbinals from dog olfactory tissue.

Individual turbinals from the right and left sides of dog olfactory tissue were removed and nerve-ending-particle preparations were prepared. (Na+ + K+)-dependent ATPase activities of the individual preparations, and the effect of several odorous compounds [including (+)- and (-)-carvone] on the (Na+ + K+)-dependent ATPase activities, were determined. The maximally stimulatory odorant concentration in the reaction mixture for the majority of odorants was found to be 1.0 mM. Matched pairs of left/right turbinals showed a lack of bilateral symmetry of response. (Na+ + K+)-dependent ATPase activities of various dog brain nerve-ending particle preparations responded only slightly to 1.0 mM odorants. The role of phospholipids in the (Na+ + K+)-dependent ATPase activity was found to be critical. Partial replacement of endogenous lipid with either synthetic phospholipids or extracted lipids resulted in changes in stimulation obtained with endogenous lipids alone.

In vitro response of ATPase activities in tissue subcellular particle preparations to a series of mono-unsaturated C18 fatty acids.

The positions of the double bond and the cis/trans configurations of six mono-unsaturated C18 fatty acids (FA) showed selectivity for inhibition and stimulation of ATPase activities of tissue homogenate fractions. The 13,000 g and 100,000 g sediments (fractions B and C respectively) of tissues homogenates were used as sources of Na+-K+ ATPase and of oligomycin-sensitive (OS) and -insensitive (OIS) Mg2+ ATPase activities. Tissue source included bovine brain and rat brain, kidney, heart and liver. Cis mono-unsaturated C18 FA caused an apparent uncoupling of mitochondrial coupling factor F1 (Mg2+ ATPase). This was indicated by the loss of oligomycin and 1,1,1-trichloro-2,2 bis (p-chlorophenyl) ethane (DDT) sensitivity in the presence of 50 microM FA (12-C18:1). Thus, a precipitous decrease in OS-Mg2+ AtPase activity of mitochondria was accompanied by an equally steep increase in OIS-Mg2+ ATPase activity. This was especially apparent in the heart tissue preparation. The uncoupling action of the FA was not observed with the trans mono-unsaturated C18 FA, Na+-K+ ATPase activity from a bovine brain nerve ending particle (B) fraction was also sensitive to 12-C18:1 FA. However, inhibitory response of Na+-K+ ATPase activity were different for OS-Mg2+ ATPase activity. The latter (OS) was not sensitive to the trans 12-C18:1, while the former (Na+-K+) was sensitive to both cis and trans forms of 12-C18:1 and inhibition appeared to be dependent on the position of the double bond.

Partial purification and characterization of a Ca(2+)-stimulated lipoxygenase from soybean seeds.

A highly purified Ca(2+)-stimulated lipoxygenase was isolated from the Hill variety of soybean seeds. Separation of Ca(2+)-stimulated lipoxygenase from lipoxygenase active in the absence of Ca(2+) (lipoxygenase-1) was readily obtained using a DEAE-cellulose column. Sample size applied to the ion exchange column was found to be critical. Both enzymes were bound to the column, although some highly active Ca(2+)-stimulated lipoxygenase eluted with buffer in the presence of bound lipoxygenase-1. Ca(2+)-stimulated lipoxygenase bound to DAAE-cellulose required the use of a NaCl gradient for elution. Ca(2+)-stimulated lipoxygenase showed an apparent isoelectric point at pH 5.90 and optimum activity at pH 7.5 and at 1.1 mM calcium. Lipoxygenase-1 was inhibited over 95% in the presence of 60 µM methyl mercuric chloride, while Ca(2+)-stimulated lipoxygenase showed a maximum of only 20% inhibition under the same conditions.