A simplified molecular method for distinguishing among species and ploidy levels in European water frogs (Pelophylax).

Western Palearctic water frogs in the genus Pelophylax are a set of morphologically similar anuran species that form hybridogenetic complexes. Fully reliable identification of species and especially of hybrid ploidy depends on karyological and molecular methods. In central Europe, native water frog populations consist of the Pelophylax esculentus complex, that is, P.

Mitochondrial genome organization and divergence in hybridizing central European waterfrogs of the Pelophylax esculentus complex (Anura, Ranidae).

Natural transfer of mitochondrial DNA has occurred between three western Palaearctic waterfrog taxa: Pelophylax lessonae, Pelophylax ridibundus and their hybridogenetic hybrid, Pelophylax kl. esculentus. The transfer is asymmetric with most P.

Kinetic properties of Pelophylax esculentus muscle FBPase.

D-Fructose-1,6-bisphosphate 1-phosphohydrolase FBPase; [EC 3.1.3.

Mononuclear and polymorphonuclear leukocytes show increased fructose-1,6-bisphosphatase activity in patients with type 1 diabetes mellitus.

The activity and localization of fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.

F-actin, beta-tubulin, aldolase, and fructose-1,6-bisphosphatase in heteropteran ovarioles--I. Immunocytochemical investigations of whole-mounted ovarioles.

The distribution of F-actin, beta-tubulin, aldolase, and fructose-1,6-bisphosphatase (FBPase) in ovarioles of four heteropteran species (Ilyocoris cimicoides, Coreus marginatus, Lygus pratensis, and Notostira elongata) was investigated biochemically and immunocytochemically. Aldolase was found to be uniformly distributed in the cytoplasm of trophocytes and follicular cells, with the highest concentration in prefollicular cells. Its concentration in follicular cells increased during differentiation and reached a peak in ovarian follicles at the stage of late choriogenesis.

Localization of chicken muscle FBPase in cardiomyocyte nuclei.

Fructose 1,6-bisphosphatase (FBPase; EC 3.1.3.

The interaction of FBPase with aldolase: a kinetic and fluorescence investigation on chicken muscle enzymes.

Fructose-1,6-bisphosphatase (FBPase; EC 3.1.3.

The effect of high dose of cortisol on glucose-6-phosphatase and fructose-1,6-bisphosphatase activity, and glucose and fructose-2,6-bisphosphate concentration in carp tissues (Cyprinus carpio L.).

The effect of a high dose of cortisol (200 mg kg(-1) body mass) on juvenile carp was investigated. The activity of glucose-6-phosphatase in liver and of fructose-1,6-bisphosphatase in liver, kidney and muscle, the serum glucose and fructose-2,6-bisphosphate concentration as well as the serum concentration of the injected hormone were measured after 24, 72 and 216 h after intraperitoneal cortisol injection. The activities of fructose-1,6-bisphosphatase in liver and kidney and glucose-6-phosphatase in liver were elevated in comparison with the control, while the fructose-1,6-bisphosphatase activity in the muscle tissue was unchanged.

Hematological effects of high dose of cortisol on the carp (Cyprinus carpio L.): cortisol effect on the carp blood.

The level of circulating cortisol and peripheral blood parameters were determined in carp age 2 years (K(2)) 24, 72, and 216 h after a single intraperitoneal injection of a high dose (200 mg x kg(-1) body wt) of hydrocortisone. The most striking effect of cortisol was manifest as a significant change in the percentage composition of leukocytes, whose number per unit volume of blood remained relatively constant. A profound lymphopenia and eosinopenia were compensated for in the general balance by an increased number of circulating promyelocytes and myelocytes as well as metamyelocytes and mature polymorphonuclear neutrophilic granulocytes.

Regulatory properties of Rana esculenta liver D-fructose-1,6-bisphosphate 1-phosphohydrolase and their comparison with properties of other vertebrate liver isoenzymes.

D-Fructose-1,6-bisphosphate 1-phosphohydrolase [EC 3.1.3.

Rana esculenta L. liver Fru-1,6-P2ase and G-6-Pase activity and Fru-2,6-P2 concentration after acclimation at 5 and 25 degrees C.

The activities of Fru-1,6-P2ase and G-6-Pase in liver and kidney of frogs acclimated at 5 and 25 degrees C and Fru-2,6-P2 level in liver were investigated. The aim of this study was to examine the effect of thermal acclimation on regulatory enzymes of gluconeogenesis and on concentration of gluconeogenesis regulator. Fru-1,6-P2ase activity in liver of frogs acclimated at 5 degrees C was 6.

Kinetic parameters of human and rabbit liver D-fructose 1,6-diphosphate 1-phosphohydrolase determined at 25 and 37 degrees C.

1. Kinetic parameters of human and rabbit liver D-fructose 1,6-diphosphate 1-phosphohydrolase (EC 3.1.