PubMed HealthSearch

Biomedical subjects

A Bedri

Publications and source records attributed to A Bedri.

5 recordsLinked to original sources

Idiopathic thrombocytopenic purpura (ITP) in Ethiopian children: clinical findings and response to therapy.

This retrospective study provides information on the clinical findings and response to therapy in Ethiopian children with idiopathic thrombocytopenic purpura. Forty-nine cases of idiopathic thrombocytopenic purpura admitted to the teaching hospital, Ethio-Swedish Children's Hospital (ESCH) in Addis Abeba, Ethiopia between January 1982 and December 1993 were studied. Among these were 31 females and 18 males with a female to male ratio of 1.9:1. The age range was three to 12 years with a mean of seven years. The commonest presenting clinical features were petechiae, epistaxis, gingival and gastro-intestinal bleeding. Twenty-nine patients were treated with prednisolone, out of whom, 27 attained absolute remission. Twenty patients were observed and managed conservatively and attained spontaneous remission. One child went on to develop chronic idiopathic thrombocytopenic purpura and underwent splenectomy after immunosuppressive treatment failure, while another child is still being followed up with recurrent episodes of thrombocytopenia and epistaxis. No mortality was noted in the review of these series of patients.

Age Distribution

6-Phosphofructo-2-kinase and fructose-2,6-bisphosphatase from Saccharomyces cerevisiae.

In permeabilized yeast cells 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase are studied during growth. It is shown that in yeast at least two fructose 2,6-bisphosphate degrading enzyme activities occur, differing in pH profile and in their substrate affinities. The activities of 6-phosphofructo-2-kinase and of fructose-2,6-bisphosphatases drop in the exponential and the transition phase while the activity of the alkaline phosphatases steadily increases. In the stationary phase the activities of 6-phosphofructo-2-kinase and of the low Km fructose-2,6-bisphosphatase increase again. Yeast 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase were purified and separated from each other. The purified 6-phosphofructo-2-kinase was found to exhibit a very high specific activity (1.3 U/mg). The enzyme is efficiently inhibited by ATP. The ATP inhibition is most pronounced at low concentrations of magnesium and fructose-6-phosphate. Phosphoenolpyruvate and sn-glycerol 3-phosphate are inhibitors of the enzyme. The high-affinity yeast fructose-2,6-bisphosphatase releases inorganic phosphate from the 2-position of fructose 2,6-bisphosphate. It displays hyperbolic kinetics towards fructose 2,6-bisphosphate (Km = 0.3 microM) and is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by sn-glycerol 3-phosphate. The enzyme is shown to be inactivated by cAMP-dependent phosphorylation and reactivated by the action of protein phosphatase 2A.

Cell Membrane Permeability

Kinetics of 6-phosphofructo-2-kinase from Saccharomyces cerevisiae: inhibition of the enzyme by ATP.

6-Phosphofructo-2-kinase (PFK-2) was purified from yeast and separated from fructose-2,6-biphosphatase (FBPase-2). The purification procedure involved polyethylene glycol fractionation followed by chromatography on DEAE-Sephacel. PFK-2 and FBPase-2 were copurified in these steps. Separation of the two enzymes resulted from Sephacryl S-300 Blue chromatography. Then, PFK-2 was chromatographed on CM-Sephadex and eluted with a gradient of KCl. Finally, PFK-2 was rechromatographed at CM-Sephadex and specifically eluted with fructose 6-phosphate. PFK-2 (specific activity 1.3 U/mg) was purified about 25,000-fold. The enzyme is inhibited by ATP which is particularly pronounced at low concentrations of magnesium and fructose 6-phosphate. Phosphoenolpyruvate and sn-glycerol 3-phosphate are inhibitors of the enzyme.

Adenosine Diphosphate

Ainhum.

Explore the source record for details and available documents.

Ainhum