Palynological characterisation of the Lower Carnian of the KEA5 borehole (Koudiat El Halfa Dome; Central Atlas, Tunisia)

In Central Tunisia, the Triassic outcrops of the Koudiat El Halfa and Rheouis Domes are mainly composed of an evaporite-dominated succession. The scarce biostratigraphic data available to date assign a Ladinian-Carnian age for the outcropping strata. The present palynological study data demonstrate an Early Carnian (Julian) age for the Triassic sediments penetrated by the KEA5 borehole in the Koudiat El Halfa Dome, which were previously considered to represent Middle Triassic. The palynological record mainly consists of Enzonalasporites vigens, Patinasporites densus, Vallasporites ignacii, Brodispora striata, Samaropollenites speciosus, Ovalipollis pseudoalatus in association with Circumpolles species such as Praecirculina granifer, Camerosporites secatus and Duplicisporites granulatus. In addition, Lagenella martini and Aulisporites astigmosus occur in the upper part of the drilled succession and their first appearance could indicate a Julian-Early Tuvalian age. These new data allow a palynostratigraphic correlation with the Rheouis Formation cropping out along the structural “North-South Axis” of Central Tunisia, particularly in the Jebel Rheouis Dome. The drilled succession can be correlated with the Black Dolostones (Tr3) and the Middle Gypsum (Tr4) members of the Rheouis Formation.     

Protein methylation in normal and cystic fibrosis fibroblasts

Human-cultured fibroblasts contain protein methylase activities. These activities were determined and the enzymatic products were identified after acid hydrolysis of the protein substrate for protein methylases I (arginine) and III (lysine) and by organic solvent extraction of the methanol produced by alkaline treatment of the protein substrate (for the protein methylase II). A methylation of histidine residues of proteins occurs in cultured fibroblasts. Protein methylase activities were unmodified in the cystic fibrosis fibroblasts as compared to the control cells.     

N-Acetylglutamate synthetase in human liver: Regulation of activity by L-Arginine and N-Acetylglutamate

A sensitive assay for the determination of N-Acetylglutamate synthetase activity in human liver has been developed. The activity was markedly stimulated by L-Arginine and inhibited by its product N-Acetylglutamate. Apparent kinetic properties were similar to those of the rat liver enzyme. This work provides the first evidence for the presence of N-Acetylglutamate synthetase activity in human.     

Effects of organic acids on the synthesis of citrulline by intact rat liver mitochondria

Citrulline synthesis, mostly regulated at the carbamoyl-phosphate synthase I (EC 6.3.4.16) step by the intramitochondrial concentration of ATP and/or N-acetylglutamate is tested with four organic acids: propionate, alpha-ketobutyrate, dipropyl-acetate and 4-pentenoate. In the presence of 10 mM succinate, as the oxidizable substrate, citrullinogenesis was only inhibited by propionate and 4-pentenoate. With 10 mM L-glutamate, a significant inhibition was observed with the four acids. After the addition of ATP and N-acetylglutamate to uncoupled mitochondria, no inhibition could be demonstrated with dipropylacetate and 4-pentenoate. However, a slight inhibition remained with propionate and alpha-ketobutyrate. When mitochondria were incubated with 10 mM L-glutamate, ATP decreased with propionate, dipropylacetate and 4-pentenoate. Under the same conditions, N-acetylglutamate synthesis was strongly inhibited by each organic acid. The decrease of N-acetylglutamate synthesis was related to the constant diminution of intramitochondrial acetyl-coenzyme A (CoA) and to the increase of propionyl-CoA with propionate and alpha-ketobutyrate. Acetyl-CoA and propionyl-CoA are respectively substrate and competitive inhibitor of the N-acetylglutamate synthase (EC 2.3.1.1). Each acid displayed its optimum inhibition at concentrations between 1 and 2 mM. At these acid concentrations, mitochondria had the lowest acetyl-CoA content and the highest propionyl-CoA content.     

Developmental changes of citrullinogenesis, mitochondrial N-acetylglutamate content and N-acetylglutamate synthetase in fetal and neonatal rats

A low citrullinogenesis (less than 60 per cent of the adult value) was observed throughout the suckling period when mitochondria isolated from newborn rat liver were incubated in vitro with L-glutamate or succinate as oxidizable substrates. The adult value was reached after weaning. From birth to weaning, intact mitochondria synthesized more citrulline when supplemented with L-glutamate than with succinate. The low citrullinogenesis could not be explained by low carbamoylphosphate synthetase-I and ornithine transcarbamoylase activities that reached adult values at birth. The decreased citrullinogenesis seen for the first three days of life seemed to be related to the low intramitochondrial concentration of N-acetylglutamate, an activator of the carbamoylphosphate synthetase-I. The concentration of this activator did not differ from that reported for adult rat liver mitochondria after the fourth day of life. The discrepancy between the normal value of N-acetylglutamate concentration and the low activity of the N-acetylglutamate synthetase (15 to 30 per cent of the adult activity) is discussed on the basis of acetyl-CoA or L-glutamate availability in mitochondria isolated from newborn or young rats.