Palliative care referral and associated outcomes among patients with cancer in the last 2 weeks of life.

Background: Palliative care (PC) improves the quality of life of patients with advanced cancer. Our aim was to describe PC referral among patients with advanced cancer, and associated outcomes in an academic medical centre.

Methods: We reviewed the medical records of 536 inpatients with cancer who had died in 2010.

Study of fatty acid specificity of sunflower phospholipase D using detergent/phospholipid micelles.

The fatty acid specificity of phospholipase D purified from germinating sunflower seeds was studied using mixed micelles with variable detergent/phospholipid ratios. The main advantage of this approach is that since the substrate is integrated in the detergent micelles, comparisons can be made between the kinetic constants of a wide range of phosphatidylcholine (PtdCho) compounds with various fatty acid contents. Phospholipase D is subject to interfacial activation as it is most active on water-insoluble substrates.

Phospholipase D from soybean (Glycine max L.) suspension-cultured cells: purification, structural and enzymatic properties.

Phospholipase D (phosphatidylcholine phosphatidohydrolase EC 3.1.4.

Purification and characterization of a fatty acyl-ester hydrolase from post-germinated sunflower seeds.

Fatty acyl-ester hydrolase was not detectable in dry sunflower seeds using various p-nitrophenyl-acyl-esters, 1,2-O-didodecyl-rac-glycero-3-glutaric acid-resorufin ester or emulsified sunflower oil as substrate. After inhibition of the seeds, acyl-ester hydrolase activity slowly developed in cotyledon extracts and was maximal after 5 days. No activity was directly measurable on oil bodies.

Lipases of the euphorbiaceae family: purification of a lipase from Euphorbia characias latex and structure-function relationships with the B chain of ricin.

A lipase from the latex of Euphorbia characias was purified using a method involving extraction with apolar solvent and adsorption chromatography on silica gel. The lipase (specific activity, 1500 international units/mg of protein) was eluted from silica gel complexes with a lipid. The main protein fraction, which had a molecular mass of 38 kDa, was inactive when dissociated from the lipid fraction.