Alternative Use of Femoral Compression System in Palliative Care: A Case Report.

Terminal hemorrhage, although relatively rare, presents a significant challenge in palliative care, necessitating effective management strategies to alleviate distress in patients and their families. This report presents the case of a 77-year-old woman with advanced vulvar squamous cell carcinoma. The patient had ulcerated groin metastases that had affected the nerve and vasculature of her left leg.

Predictors of obsessive-compulsive symptomology: mind wandering about the past and future.

Purpose: Obsessive and compulsive tendencies are known to occur in the general population and involve worry around specific concerns (obsessions) and an urge to resolve the concern with thoughts or behaviours (compulsions). Spontaneous, but not deliberate, mind wandering experiences (when attention turns to internal mentation), have been found to predict obsessive- compulsive tendencies [Seli, P., Risko, E.

Ethical behaviors of psychologists: changes since 1987.

Licensed psychologists (n = 92) in Illinois were surveyed regarding the frequency with which they engage in 82 behaviors of varying ethical appropriateness. For about one-third of the behaviors studied, results differed significantly from a similar national survey published in 1987, such that the current sample reported never engaging in the behavior more frequently than did the previous sample. These differences may be due to increased involvement of managed care in professional practice, the revised ethical code, or regional or sampling factors.

Glucagon activates mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase in vivo by decreasing the extent of succinylation of the enzyme.

1. 3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase (EC 4.1.

Treatment of rats with glucagon or mannoheptulose increases mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase activity and decreases succinyl-CoA content in liver.

1. The activity of 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase (EC 4.1.

Purification and properties of the soluble carnitine palmitoyltransferase from bovine liver mitochondria.

A new carnitine palmitoyltransferase (CPT) was purified to homogeneity from bovine liver mitochondria which were 96% free of peroxisomal contamination, as judged by catalase and glutamate dehydrogenase activities. The enzyme is easily removed from mitochondria, without the use of detergent. It is monomeric (Mr 63,500), unlike other preparations of CPT from mitochondria, and is most active with myristoyl-CoA and palmitoyl-CoA.

Aggregation of submitochondrial particles by heparin and its application to the study of carnitine transport.

A novel technique for the separation of submitochondrial particles from the external medium, an essential procedure in transport studies, was devised. Very low concentrations of heparin (5-10 micrograms/ml) aggregate the particles and permit their rapid sedimentation in a micro-centrifuge. The transfer of activated fatty acids into mitochondria for oxidation depends on the exchange of matrix carnitine for external fatty-acylcarnitine.

Succinylation and inactivation of 3-hydroxy-3-methylglutaryl-CoA synthase by succinyl-CoA and its possible relevance to the control of ketogenesis.

Succinyl-CoA (3-carboxypropionyl-CoA) inactivates ox liver mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (EC 4.1.3.

Limited proteolysis of pig liver CoA synthase: evidence for subunit identity.

The bifunctional enzyme CoA synthase can be nicked by trypsin without loss of its activities. The original dimer of subunit Mr approx. 61 000 yields fragments of Mr 41 000 and 22 000 as seen on gel electrophoresis in the presence of SDS, but the nicked enzyme retains the native Mr of 118 000.

3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Properties of its acetyl derivative.

Ox liver mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (EC 4.1.3.

3-Hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver. Purification, molecular and catalytic properties.

Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (EC 4.1.3.

A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinase.

Pantetheine phosphate adenylyltransferase (EC 2.7.7.

Preparation of bromo[1-14C]acetyl-coenzyme A as an affinity label for acetyl-coenzyme A binding sites.

Bromo[1-14C]acetyl-CoA has been prepared from CoASH and the N-hydroxysuccinimide ester of bromo[1-14C]acetic acid, and unlabeled bromoacetyl-CoA by reaction of CoASH with bromoacetyl bromide. The products were purified by high-pressure liquid chromatography. Purified bromoacetyl-CoA was characterized, and found to be a potent alkylating agent with a substantial stability in aqueous solution: it decomposed at 30 degrees C and pH 6.

Some properties of 3-hydroxy-3-methylglutaryl-coenzyme A synthase from ox liver.

Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (EC 4.1.3.

Mitochondrial transport processes and oxidation of NADH by hypotonically-treated boar spermatozoa.

1. After hypotonic treatment spermatozoa have metabolic characteristics of mitochondria isolated from other cells. Ejaculated boar spermatozoa treated in this way can oxidise external NADH via both a lactate-pyruvate shuttle and a malate-aspartate cycle; this oxidation is coupled to the phosphorylation of ADP.

Deacylation of acetyl-coenzyme A and acetylcarnitine by liver preparations.

The breakdown of acetylcarnitine catalysed by extracts of rat and sheep liver was completely abolished by Sephadex G-25 gel filtration, whereas the hydrolysis of acetyl-CoA was unaffected. Acetyl-CoA and CoA acted catalytically in restoring the ability of Sephadex-treated extracts to break down acetylcarnitine, which was therefore not due to an acetylcarnitine hydrolase but to the sequential action of carnitine acetyltransferase and acetyl-CoA hydrolase. Some 75% of the acetyl-CoA hydrolase activity of sheep liver was localized in the mitochondrial fraction.