Streptosporangium anatoliense sp. nov., isolated from soil in Turkey

A novel actinobacterium, strain N9999^T, was isolated from soil and its taxonomic position determined using a polyphasic approach. The organism formed abundant aerial hyphae that differentiated into spherical spore vesicles. The cell wall contained meso-diaminopimelic acid; the whole-cell sugars were galactose, glucose, mannose, madurose and ribose; the predominant menaquinones MK-9 (H₂) and MK-9 (H₄); the major phospholipids phosphatidylethanolamine, diphosphatidylglycerol, a phosphaglycolipid and phosphatidylinositol mannosides; while the cellular fatty acids were rich in iso-C_14:0, C_15:0, cis-9-C_17:1, iso-C_16:0 and 10-methyl C_17:0 components. Phylogenetic analyses based on an almost complete 16S rRNA gene sequence indicated that strain N9999^T was closely related to a group that consisted of Streptosporangium pseudovulgare DSM 43181^T and Streptosporangium nondiastaticum DSM 43848^T. However, DNA–DNA relatedness and phenotypic data demonstrated that strain N9999^T was clearly distinguished from all closely related Streptosporangium species. The combined genotypic and phenotypic data demonstrate conclusively that the isolate should be classified as a new species of Streptosporangium.     

Three new G6PD variants,G6PD Adana,G6PD Samandağ, and G6PD Balcali in Çukurova,Turkey

Summary Glucose-6-phosphate dehydrogenase (G6PD) enzyme from cases known to be completely or mildly deficient were analyzed. The enzymes were purified from blood samples by utilizing DEAE-52 cellulose pH 7.0 column chromatography and ammonium sulphate precipitation. Biochemical and electrophoretic properties of G6PD were studied in these partially purified enzymes. In this study wer report three new variants from Çukurova, named Adana, Samanda, and Balcali. Variant I (G6PD Adana) had a high K_m for G6P (210 M) and NADP (13M). Utilization of 2d-G6P was 38%. It had a slow electrophoretic mobility, a biphasic pH optimum curve, and abnormal heat stability. Variant II (G6PD Samanda) had a low K_m for G6P (25M) and a high K_m for NADP (18M). The rate of utilization of 2d-G6P was normal. G6PD Samanda deviated from the normal enzyme by its biphasic pH optimum curve and its slow electrophoretic mobility. Variant III (G6PD-Balcali) had a normal K_m G6P, NADP and rate of utilization of 2d-G6P. However, it showed a biphasic pH optimum curve and slow electrophoretic mobility.