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Biomedical subjects

R Calmes

Publications and source records attributed to R Calmes.

10 recordsLinked to original sources
PubMed1996

Kinetics of amino acid and glucose absorption following pancreatic diversion in the pig.

An experiment was conducted in the pig to determine the consequences of deprivation of exocrine pancreatic secretion on the composition and quantity of nutrients absorbed after intake of a balanced diet. Five growing pigs (53.8 kg body weight) were fitted with permanent catheters in the portal vein and the carotid artery and with an electromagnetic flow probe around the portal vein to measure the exchanges between the blood and the intestinal lumen. They were also fitted with a permanent catheter in the duct of Wirsung to educe the exocrine pancreatic secretion and another one in the duodenum in order to reintroduce it. In each animal, glucose, amino-N and amino acid absorption as well as insulin and glucagon production were measured over a period of 10 h after the meal (semi-purified diet based on purified starch and containing 180 g fish meal/kg, DM content of the meal 731 g), either in the presence of pancreatic juice (group C: immediate reintroduction), or in the absence of pancreatic juice (group D: deprivation). The deprivation of pancreatic juice provoked a marked depression in the absorption of glucose (D 67.9 (SEM 27.9) g/10 h, C 437.7 (SEM 39.5) g/10 h, P < 0.001), and of amino-N (D 7.55 (SEM 0.54) g/10 h, C 15.80 (SEM 0.79) g/10 h, P < 0.001). The composition of the mixture of amino acids in the portal blood was only slightly modified: only the levels of histidine (P < 0.05) and of valine (P < 0.06, NS) decreased in the absence of pancreatic juice. Insulin production was much lower (by 64%, P < 0.05) in the absence of pancreatic juice whereas that of glucagon was not affected.

Amino Acids↗
PubMed1984

[Effect of a short-term protein-free diet on endogenous nitrogen secretion: exocrine pancreas secretion in the pig].

A protein-free diet is often used in animal experimentation to estimate the amount of total endogenous nitrogen secreted by the organism. To test the validity of this technique, we carried out a study on pigs describing the short-term (8-day) effect of a protein-free diet on exocrine pancreas nitrogen secretion; this nitrogen was considered as representative of total endogenous nitrogen. After 11 pigs had been adapted to a balanced diet (14% protein), they were chronically fistulated in the pancreatic duct and duodenum. Pancreatic secretion and its various parameters (volume, total protein and chymotrypsin, trypsin, amylase and lipase activities) were measured over a first experimental period of 4 days, during which the pigs continued to receive the balanced diet, and over a second experimental period of 8 days during which they were given a protein-free diet. The results show that the amount of pancreatic protein did not change during the period the protein-free diet was given. After 2 days, chymotrypsin specific activity dropped, while amylase and lipase specific activities decreased little and slowly after 6 days. However, for short-term experiments, the protein-free diet proved to be an adequate technique for determining the production of total endogenous nitrogen in the digestion tract.

Amino Acids↗
PubMed1982

A case study of a nontraditional basic science curriculum.

This article presents a critical analysis of the ten-year experience of the Department of Oral Biology of the University of Kentucky College of Dentistry with a nontraditional basic science curriculum. The factors that led to the adoption of this curriculum are outlined, and its effects on students, faculty, and the college's administration are described. The pitfalls inherent in this approach and in the individualized self-instructional format for teaching the basic sciences to dental students are discussed. This critical evaluation is aimed at providing information for those contemplating similar sweeping curricular changes in the future to enable them to make rational decisions and to help them predict the effects of such changes on the educational program.

Curriculum↗
PubMed1980

Energy metabolism in Capnocytophaga ochracea.

Among the microflora of the gingival sulcus are members of the genus Capnocytophaga which have been implicated as possible etiological agents of juvenile periodontitis and systemic infectious diseases. In this study, the pathway used by C. ochracea strain 25 for generating energy from glucose was investigated. When grown in a complex medium supplemented with glucose and NaHCO(3), the major end products formed were acetate (4.6 mmol), succinate (11.0 mmol), pyruvate (4.3 mmol), and oxalacetate (3.6 mmol), and the molar growth yield was 58. Addition of yeast extract to the growth medium caused (i) an increase in acetate (9.2 mmol) and succinate (14.3 mmol), (ii) a decrease in pyruvate (0 mmol) and oxalacetate (1.1 mmol), and (iii) the molar growth yield increased to 75. Glucose was transported by a phosphoenolpyruvate:phosphotransferase system and then catabolized to phosphoenolpyruvate by enzymes of the Embden-Meyerhof-Parnas pathway. No activities were detected for the key enzymes of the Warburg-Dickens, Entner-Douderoff, or hexose phosphoketolase pathways. During growth in the yeast extract-supplemented medium, approximately 37% of the phosphoenolpyruvate carbon was converted to acetate by pyruvate kinase, a pyruvate-decarboxylating enzyme activity, and acetate kinase; the remaining 63% was converted to succinate via phosphoenolpyruvate carboxykinase, malate dehydrogenase, fumarate hydratase, and fumarate reductase.

Adenosine Triphosphate↗
PubMed1979

Regulation of lactose catabolism in Streptococcus mutans: purification and regulatory properties of phospho-beta-galactosidase.

Phospho-beta-galactosidase (P-beta-gal), the enzyme which catalyzes the first step in the metabolism of intracellular lactose phosphate, occurred at high specific activity in the cytoplasm in 12 of 13 strains of streptococcus mutans grown on lactose but not other carbon sources. The P-beta-gal from S. mutans SL1 was purified 13-fold using diethylaminoethyl-cellulose ion exchange and agarose A--0.5 M molecular exclusion column chromatography. The molecualr weight of the enzyme was estimated to be 40,000, and its pH optimum was 6.5 in three different buffer systems. P-beta-gal activity was inhibited by Co2+, Zn2+, and Cu2+, but other cations, ethylenediaminetetraacetic acid, orthophosphate, and fluoride had no effect upon enzyme activity. The kinetic response of P-beta-gal to a model substrate, o-nitrophenyl-beta-D-galactopyranoside-6-phosphate, obeyed Michaelis-Menten kinetics, and the Km for this substrate was 0.19 mM. In addition to being under genetic control, P-beta-gal activity was regulated by a number of biologically active metabolites. Enzyme activity was inhibited in a sigmoidal fashion by phosphoenolpyruvate. The M 0.5 V value for phosphoenolpyruvate was 2.8 mM, and the Hill coefficient (n) was 3. In addition, P-beta-gal exhibited strong inhibition by ATP, galactose-6-phosphate, and glucose-6-phosphate. In contrast to inhibition of P-beta-gal activity by phosphoenolpyruvate, the inhibition exerted by ATP, galactose-6-phosphate, and glucose-6-phosphate obeyed classical Michaelis-Menten kinetics; the Ki values for these inhibitors were 0.55, 1.6, and 4.0 mM, respectively.

Adenosine Triphosphate↗
PubMed1978

Involvement of phosphoenolpyruvate in the catabolism of caries-conducive disaccharides by Streptococcus mutans: lactose transport.

The mechanisms for transport and hydrolysis of lactose were investigated in five cariogenic strains (HS6, AHT, FA1, NCTC 10449, and SL1) representing the four serogenetic groups of Streptococcus mutans. The systems for transport and hydrolysis of lactose had the characteristics of a phosphoenolpyruvate (PEP)-dependent lactose (Lac) phosphotransferase (PT) system and phospho-beta-galactosidase (P-beta-gal), respectively, in all strains tested, except strain HS6. Decryptified cells required PEP and Mg(2+) for transport of the non-metabolizable model beta-galactosides o-nitrophenyl-beta-d-galactopyranoside (ONPG) and thiomethyl-beta-d-galactopyranoside (TMG). Substitution of 2-phosphoglycerate (2-PG) for PEP also stimulated the Lac PT system. Other potential high-energy phosphate donors (adenosine tri-, di-, and monophosphates and guanosine triphosphate) did not stimulate the Lac PT system. Sodium fluoride had no effect upon the PEP-dependent Lac PT system in decryptified cells with PEP as the energy source; however, when 2-PG was used as the energy source, F(-) inhibited ONPG phosphorylation. With intact cells which must generate PEP endogenously, the presence of F(-) in concentration >/= 10 mM completely inhibited the Lac PT system, presumably through inhibition of 2-PG hydrolyase (EC 4.2.1.11; enolase). Both intact and decryptified cells accumulated a phosphorylated derivative of TMG that behaved chromatographically as TMG-phosphate. After alkaline phosphatase treatment, the derivative had an R(f) identical to that of TMG. No beta-galactosidase (beta-gal) activity was detected with ONPG as the substrate; hydrolysis occurred only when ONPG-6-phosphate was supplied as the substrate. Strain HS6 apparently transported lactose by an active transport-type system in which the accumulated intracellular product was the free disaccharide based on the following criteria: (i) ONPG transport and hydrolysis in decryptified cells was not stimulated by PEP; (ii) ONPG hydrolysis occurred in the absence of PEP; and (iii) ONPG-6-phosphate was not hydrolyzed. These data indicate that, in all strains tested except strain HS6, lactose transport was mediated by a PEP-dependent Lac PT system, resulting in accumulation of lactose-phosphate that was hydrolyzed by an enzyme similar to the P-beta-gal of group N streptococci and Staphylococcus aureus; conversely, strain HS6 transported and hydrolyzed lactose by a PEP-independent transport system and beta-gal, respectively.

Biological Transport↗
PubMed1976

Fatty acid transport by the lipophilic bacterium Nocardia asteroides.

Hexadecanoate was translocated in Nocardia asteroides by a constitutive transport system(s), which transported short, medium, and long-chain fatty acids. Inhibition of hexadenocanoate transport by homologues suggested that at least two systems are present: one specific for short-chain fatty acids and the other specific for medium- and long-chain fatty acids. Saturation kinetics typical of a carrier-mediated transport system (Kt = 870 muM)were observed, and concentration of fatty acids against a gradient was achieved. Inhibitor studies indicated that free sulfhydryl groups, a functional respiratory chain, and energy are required for translocation. Efflux of [14C]hexadecanoate in the presence of excess unlabeled hexadecanoate or 2,4-dinitrophenol and the cytoplasmic localization of acyl-coenzyme A synthetase (acid:coenzyme A ligase [adenosine monophosphate]; EC 6.2.1.3) (Calmes and Deal, 1973) are consistent with the hypothesis that fatty acids are transported and released intracellularly as free fatty acids.

Adsorption↗
PubMed1973

Fatty acid activation by a lipophilic bacterium.

Cell-free extracts of Nocardia asteroides activated saturated fatty acids from octanoate to octadecanoate, plus docosanoate; maximal activation occurred with dodecanoate. No activation of short-chain fatty acids was observed. The activating enzyme, characterized as an acyl-coenzyme A (Co A) synthetase (acid: Co A ligase [adenosine monophosphate]; EC 6.2.1.3), was localized in the cytoplasm of the cells and had absolute requirements for Co A, adenosine 5'-triphosphate, and Mg(2+). Kinetic data suggested that N. asteroides possessed at least two synthetases: one specific for short-chain fatty acids, and the other specific for medium- and long-chain fatty acids.

Adenosine Monophosphate↗