Factors influencing self-management in patients with type 2 diabetes: a quantitative systematic review protocol.

Aim: To describe a protocol for a quantitative systematic review, to identify critique and summarize factors that influence self-management education.

Background: Self-management education enables patients to manage their condition successfully and it is associated with better self-care, good control over lifestyle and leading the best possible quality of life, notwithstanding the presence of a chronic disease. Type II Diabetes is a chronic disease that requires lifestyle adjustments and disease management to keep glycaemia and long-term complications under control.

An extracellular endodeoxyribonuclease from Streptomyces aureofaciens.

Several extracellular DNases were detected after cultivation of Streptomyces aureofaciens B96 under submerged conditions. These DNases are nutritionally regulated and high content of amino acid nitrogen in cultivation medium repress their production. By varying cultivation conditions, there remained only two extracellular nuclease activities.

Lag period of 14CO2 evolution from dioctyl sulpho[2,3-14C]succinate in relation to adaptation of bacterium, Comamonas terrigena, to dialkyl esters of sulphosuccinate.

Comamonas terrigena, strain N3H, which was isolated from soil polluted with crude oil products, degraded dioctyl sulphosuccinate, a synthetic commercial surfactant. The primary degradation of this compound, the cleavage of ester bonds between octyl groups and sulphosuccinate, lasted significantly shorter time than the subsequent breakdown of the sulphosuccinate moiety of dioctyl sulpho[2,3-(14)C]succinate. (14)CO(2) evolution had a significant shorter lag period with cells in Tris/phosphate medium, without inorganic sulphate and adapted to surfactant, than unadapted cells.

Crystal structure reveals two alternative conformations in the active site of ribonuclease Sa2.

Three different strains of Streptomyces aureofaciens produce the homologous ribonucleases Sa, Sa2 and Sa3. The crystal structures of ribonuclease Sa (RNase Sa) and its complexes with mononucleotides have previously been reported at high resolution. Here, the structures of two crystal forms (I and II) of ribonuclease Sa2 (RNase Sa2) are presented at 1.