Effect of Spirulina platensis biomass on the growth of lactic acid bacteria in milk

The stimulatory effect of aqueous suspensions of Spirulina platensis dry biomass extracted at pH 6.8 and 5.5 was studied on four lactic acid bacteria (LAB) grown in milk. The addition of dry S. platensis to milk (6 mg/ml) stimulated growth of Lactococcus lactis by 27%. The growth of other strains was also promoted. This revised version was published online in July 2006 with corrections to the Cover Date.     

Concerted regulation of free arachidonic acid and hormone-induced steroid synthesis by acyl-CoA thioesterases and acyl-CoA synthetases in adrenal cells.

Although the role of arachidonic acid (AA) in the regulation of steroidogenesis is well documented, the mechanism for AA release is not clear. Therefore, the aim of this study was to characterize the role of an acyl-CoA thioesterase (ARTISt) and an acyl-CoA synthetase as members of an alternative pathway in the regulation of the intracellular levels of AA in steroidogenesis. Purified recombinant ARTISt releases AA from arachidonoyl-CoA (AA-CoA) with a Km of 2 micro m. Antibodies raised against recombinant acyl-CoA thioesterase recognize the endogenous protein in both adrenal tissue and Y1 adrenal tumor cells by immunohistochemistry and immunocytochemistry and Western blot. Stimulation of Y1 cells with ACTH significantly stimulated endogenous mitochondrial thioesterases activity (1.8-fold). Nordihydroguaiaretic acid (NDGA), an inhibitor of AA release known to affect steroidogenesis, affects the in vitro activity of recombinant ARTISt and also the endogenous mitochondrial acyl-CoA thioesterases. ACTH-stimulated steroid synthesis in Y1 cells was significantly inhibited by a synergistic effect of NDGA and triacsin C an inhibitor of the AA-CoA synthetase. The apparent IC50 for NDGA was reduced from 50 micro m to 25, 7.5 and 4.5 micro m in the presence of 0.1, 0.5 and 2 micro m triacsin C, respectively. Our results strongly support the existence of a new pathway of AA release that operates in the regulation of steroid synthesis in adrenal cells.     

Genbank accession #: 133708

Plant Molecular Biology -     

Blood biochemistry values of sheep (Ovis aries ligeriensis)

1. Analysis of biochemical parameters were carried out on material pooled from 30 female sheep (Ovis aries ligeriensis). 2. The values determined were for the common metabolites and enzymes utilized for specific studies in general metabolism (urea, glucose, cholesterol, lipids, bilirubin, uric acid, creatinine, alkaline phosphatase, GOT, GPT, LDH, LAP, CGT, CK and amylase). 3. Results of these studies were compared with values from normal human adults. 4. The differences obtained in human and sheep ranges can be explained by the different physiology of the two species. 5. This study gives values for the sheep as an experimental animal in biomedical research.     

Properties and function of malate enzyme from Dicentrarchus labrax L. liver

Malate enzyme (L-malate:NADP+ oxidoreductase (oxaloacetate decarboxylating, EC 1.1.1.40) has been purified from Dicentrarchus labrax liver to 99% homogeneity by gel filtration, anion exchange and affinity chromatographies. The apparent molecular weight was estimated by gel filtration chromatography to be 148,000. Analysis of the enzyme on sodium dodecyl sulphate polyacrylamide disc gel electrophoresis was shown to be a tetrameric protein. The purified enzyme showed a pH optimum 8.5 (Tris-HCl buffer) and required bivalent cations for catalysis. The temperature-activity relationship for the enzyme showed broken Arrhenius plots with inflexions at 15 and 40 degrees C. Kinetic properties and the effects of some metabolites related to L-malate are studied.