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Biomedical subjects

T Yamane

Publications and source records attributed to T Yamane.

At least 559 records · Page 31Linked to original sources
PubMed1979

Protein requirement of laying Japanese quail.

1. Two feeding experiments were conducted to determine the crude protein requirement of laying Japanese quail. Birds were fed to provide 293 kJ ME and 2, 3, 4, 5, 6 or 7 g protein/d. 2. As protein intake increased from 2 to 5 g egg production increased. 3. Quadratic relationships between protein intake and egg production and protein intake and egg weight were derived. 4. To maintain a production of 90 eggs/100 bird d and an egg weight of 9.3 g required 4.9 g protein and approximately 264 kJ ME/d.

Animals↗
PubMed1979

Extramedullary plasmacytoma of the gastrointestinal tract in a renal transplant recipient.

A case of gastrointestional plasmacytoma found in a renal transplant recipient is described. Immunohistochemical study using immunoglobulin-enzyme bridge technique demonstrated IgA and k-type light chains in the majority of plasma cells infiltrated in the stomach. Pathological investigation revealed multiple similar tumors in the ileum, cecum and ascending colon suggesting a plasmacytoma of multicentric gastrointestinal origin. The pathogenesis of plasma cell tumors is briefly discussed with regard to organ transplantation.

Adult↗
PubMed1978

On the measurement of pH in Escherichia coli by 31P nuclear magnetic resonance.

The 31P high resolution NMR spectra of concentrated suspensions of Escherichia coli cells have been measured at 145.8 MHz. The position of the orthophosphate resonance is used as a measure of internal and external pH. In accord with Paddan, Zilberstein and Rottenberg ((1976) Eur. J. Biochem. 63, 533--541) it is shown that when properly energized the internal pH is 7.5 +/- 0.1. By synchronizing the NMR data acquisition with 3-s bursts of O2 it is possible to measure the internal pH with a time resolution of about 1 s. It is shown that at 20 degrees C the pH remains constant for times longer than 15 s after the oxygen is discontinued and it decays in several minutes.

Escherichia coli↗
PubMed1978

Kinetics of the 580-nm ultrafast bacteriorhodopsin transient.

We have observed, by low-temperature picosecond spectroscopy, a photo-induced transient at 580 nm in light-adapted bacteriorhodopsin. The transient was characterized by bleaching in the 550-585-nm regions within 6 ps and recovery in approximately 20 ps. The spectral intensity of the transient is found to be enhanced at lower temperatures, and the lifetime slightly elongated.

Bacteriorhodopsins↗
PubMed1978

Phosphate metabolites in lymphoid, Friend erythroleukemia, and HeLa cells observed by high-resolution 31P nuclear magnetic resonance.

High-resolution phosphorus-31 nuclear magnetic resonance spectra were observed for cell lines from mammalian sources: lymphoid cells, Friend erythroleukemia cells, and HeLa cells. Some phosphate metabolites were identified and their concentrations were found to vary among the different cell lines. ATP/ADP ratios could be measured in the living cells. The phospholipid metabolites phosphorylcholine and phosphorylethanolamine and their glyceryl esters were present in relatively high concentrations in the cells, but their ratios varied considerably. Also, a high concentration of an unidentified diphosphodiester compound was observed in the Friend erythroleukemia and HeLa cells. No appreciable pH gradient across the cell membrance was observed in these three mammalian cell lines, in contrast to the large pH gradient detected in microorganisms.

Adenosine Diphosphate↗
PubMed1977

31P nuclear magnetic resonance studies of Ehrlich ascites tumor cells.

High-resolution 31P nuclear magnetic resonance spectra at 145.7 MHz are reported for intact Ehrlich ascites tumor cells and their perchloric acid extracts. In the extracts it was possible to assign resonances to fructose 1,6-bisphosphates, dihydroxyacetone phosphate, ATP, ADP, AMP, Pi, NAD+, phosphorylcholine, glycero-3-phosphorylcholine, glycero-3-phosphorylethanolamine, and glyceraldehyde 3-phosphate from their chemical shifts, pH behavior, and spin couplings. All but glyceraldehyde 3-phosphate were observed and assigned in the intact cells. It was possible to show that the hydrolysis of fructose 1,6-bisphosphate to dihydroxyacetone phosphate and glyceraldehyde 3-phosphate is in equilibrium, that the dihydroxyacetone phosphate leads to glyceraldehyde 3-phosphate reaction is not, and that in the intact cell without added oxygen or glucose the reaction 2ADP in equilibrium ATP + AMP is in equilibrium. From the known pH dependence of the Pi resonance it was possible to show that during aerobic or anerobic glycolysis the difference between intracellular and extracellular pH values was less than 0.2 pH units. Upon oxygenation the ATP concentration increased while the ADP concentration fell. Introducing deoxyglucose depleted the ATP and resulted in an AMP signal and one from deoxyglucose 6-phosphate, which is transported and phosphorylated but not catabolized.

Adenine Nucleotides↗
PubMed1977

High-resolution 31P nuclear magnetic resonance studies of metabolism in aerobic Escherichia coli cells.

31P nuclear magnetic resonance spectra at 145.7 MHZ were obtained of concentrated suspensions of E. coli cells. The position of the Pi resonance was used to determine the pH, and in most experiments it was possible to distinguish the intracellular (pHin) and extracellular (pHex) values. During respiration pHin approached 7.55, while pHex varied from 6.0 to 8.0. With succinate as a carbon source and in a N2 environment, pHin - pHex. Upon addition of glucose, pHin greater than pHex. In the presence of an ATPase (adenosinetriphosphatase; ATP phosphohydrolase; EC 3.6.1.3) inhibitor dicyclohexylcarbodiimide, pHin remained equal to pHex even in the presence of glucose. In other experiments, oxygenation brought pHin above pHex even in the presence of dicyclohexylcarbodiimide. These experiments are consistent with Mitchell's hypothesis that, first, delta pH can be created by the reversal of the ATPase reaction and, second, that protons are pumped outward during respiration. In addition to Pi, about 10 more resonances were resolved, several of which were assigned to different phosphate metabolites.

Adenosine Triphosphatases↗
PubMed1977

Experimental evidence for kinetic proofreading in the aminoacylation of tRNA by synthetase.

The enzymatic aminoacylation of tRNA can be viewed as a means of proofreading either the amino acid or the tRNA or both. We have conducted further experimental tests of kinetic proofreading in discriminating between cognate and noncognate amino acids and tRNAs as follows: (formula: see text). In cases (i) and (ii) the amino acids are proofread, in cases (iii) and (iv) the tRNA is proofread, and in case (v), both the amino acid and the tRNA are proofread. ATP consumed per acylation was 400, 1.5, 40, 25, and 1000, respectively. High ATP/aminoacylation ratios are diagnostic for kinetic proofreading.

Amino Acyl-tRNA Synthetases↗
PubMed1977

Demonstration of a tertiary interaction in solution between the extra arm and the D-stem in two different transfer RNA's by NMR.

According to the X-ray structure of yeast tRNAPhe at 2.5 A resolution, a hydrogen bond is formed between m7G46 and G22. By removal of this m7G46-residue we demonstrate that this interaction is present in solution as well. Comparison of the 1H 360 MHz NMR spectra of intact yeast tRNAPhe and its m7G-excised derivative locates the position of this tertiary H-bond at 12.5 ppm downfield from DSS. Additional evidence for the presence of this interaction in solution comes from a comparison of 1H NMR spectra of E. coli tRNAf1Met and E. coli tRNAf3Met, which differ only in a single position in the extra arm. In tRNAf3Met residue 47 is a m7G-residue, whereas in tRNAf3Met it is A, resulting in the absence of the m7G47 - G23 - C13 triple interaction, characteristic of tRNAf1Met. The resonance position of this tertiary interaction in tRNAf1Met is located around -13.6 ppm, a chemical shift difference of 1.1 ppm with respect to the position observed for tRNAPhe. The origin of this chemical shift difference is discussed in relation to the structure of their respective augmented D-helices.

Escherichia coli↗