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PubMed1991

Dose effects of cholecystokinin and acetylcholine on phosphorus compounds and secretory responses in isolated perfused pancreas of rat.

Phosphorus nuclear magnetic resonance (31P NMR) spectroscopy was used to study energy supply for protein secretion in the isolated perfused rat pancreas. Stimulation with cholecystokinin (CCK-8) increased fluid secretion and protein output. With 10pM of CCK-8, the tissue contents of ATP, inorganic phosphate (Pi), and creatine phosphate (PCr) remained unchanged. With 100pM of CCK-8, which induced the maximum response in fluid secretion and protein output, Pi increased slightly, ATP and PCr remained almost unchanged. A high dose of CCK-8 (1 nM) suppressed the fluid and protein secretory rates, decreased ATP, and increased Pi significantly, but PCr showed a tendency of increase. Significant changes in ATP and Pi occurred on withdrawal of CCK-8 (1 nM), suggesting activation of ATP hydrolysis for recovery from secretory suppression. During stimulation with 0.1, 0.3, and 3.0 microM of acetylcholine, the similar dose-dependent response was observed in the secretion and the phosphorus metabolism. The present study demonstrated that cytosolic energy metabolism for secretory responses in the pancreas is low and the Lohmann reaction showed less contribution than in the salivary gland. The findings suggest that the energy supply for protein secretion may be cytosolic diffusion of ATP and that the Lohmann reaction system may contribute to synthesis and storing of secretory protein at resting state.

Acetylcholine↗
PubMed2000

Synthesis of an Isolable Diphosphaisobenzene and a Stable Cyclic Allene with Six Ring Atoms Phosphorus Compounds, Part 147. This work was supported by the Fonds der Chemischen Industrie and the Deutsche Forschungsgemeinschaft (Graduate College "Phosphorus chemistry as link between different chemical disciplines"). Part 146: C. Peters, F. Tabellion, A. Nachbauer, U. Fischbeck, F. Preuss, M. Regitz, Organometallics 2000, in press.

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Journal Article↗
PubMed1957

The effect of dinitrophenol, hypoxaemia and ischaemia on the phosphorus compounds of the dog heart.

The results reported in this paper indicate that dinitrophenol acts directly on the isolated heart, increasing its metabolic rate. It also produces heart failure associated with a low phosphocreatine content of the muscle but with no change in adenosine triphosphate, which may or may not be due to a relative hypoxia of the cardiac tissue. Experimental arterial hypoxaemia, if severe, produces a similar picture of heart failure with a decrease in phosphocreatine and no change in adenosine triphosphate. Ligation of the coronary arteries results in disappearance of the major part of the phosphocreatine within a few minutes regardless of whether or not ventricular fibrillation ensues; the adenosine triphosphate remains unchanged.

Adenosine Triphosphate↗
PubMed2004

Synthesis and structural characterization of trivalent amino acid derived chiral phosphorus compounds.

Reaction of the N-toluenesulfonyl derivatives of (S)-alanine, phenylalanine, and valine (4-6) with PhPCl(2) gave in high yield the 4-methyl, benzyl, and isopropyl derivatives (7-9) of 2-phenyl-1-p-toluenesulfonyl-1,3,2-oxazaphospholidin-5-one. The ratios of the (2S,4S)/(2R,4S) diastereomers (cis/trans isomers) were 1:1, 2:1, and 10:1 for the methyl, benzyl, and isopropyl derivatives 7a,b, 8a,b, and 9a,b, respectively. For 7a,b, both isomers could be crystallized, but for the others only the major isomers were isolable. The X-ray crystal structure of 9a shows that the isopropyl and phenyl groups are mutually cis and that the tolyl moiety is oriented s-trans to both the isopropyl and phenyl groups. Reaction of 6 with Cl(2)PCH(2)CH(2)PCl(2) (10) gave a 56:38:7 mixture of the cis/cis, cis/trans, and trans/trans diphosphorus heterocycles 11a-c. The major isomer could be crystallized and isolated free of the other diastereomers. Reaction of 6 with EtPCl(2) gave a 6:1 mixture of cis/trans isomers of the ethyl-substituted heterocycles 12a,b as an inseparable oil but allowed confirmation of the structure of 11a. Slow epimerization at phosphorus may occur by inversion but more likely by ring opening/closure, since 7b, 9a, and 11a give rise upon standing in solution to mixtures containing starting material and 7a, 9b, and 11b, respectively, along with the free amino acid derivatives 4 and 6. The NMR spectra, and in particular the coupling constants between the alpha-hydrogen atom of the amino acid moiety and phosphorus, were used to establish the identities of the cis and trans isomers. Reaction of 9a with (THF)W(CO)(5) gave the phosphorus-ligated adduct (9a)W(CO)(5) (13), and the IR spectrum of this complex shows that 9a is a strongly electron-withdrawing ligand. The geometry of the sulfonamide moiety is discussed in detail, as are the (1)H NMR coupling constants. The data are consistent with the presence of little steric interaction between the cis isopropyl and phosphorus substituent in 9a, 11a, and 12a and orientation of the tolyl moiety s-cis to the isopropyl group in 9b, 12b, and 13.

Amino Acids↗
PubMed1978

Complexes of trivalent oxygenated phosphorus compounds with cytochrome P-450 and cytochrome P-420: the origin of double Soret spectra.

Trivalent oxygenated phosphorus ligands include alkyl and aryl phosphites, (RO)3P, phosphonites, (RO)2PR, and phosphinites, ROPR2. All such compounds tested, with the exception of triphenyl phosphite, interact with ferrous cytochrome P-450 and its denatured form, cytochrome P-420, to produce complexes having two peaks in the Soret region of their optical difference spectra. Careful evaluation of these spectra indicate that they arise for different reasons for each of the two cytochromes. Clear evidence shows that cytochrome P-450 is not denatured by these ligands. The high affinity of these ligands for heme iron is indicated by small Ks values. The experimental results are used to substantiate a theory of the origin of microsomal double Soret spectra and the nature of the environments available for microsomal cytochromes P-450 and P-420.

Animals↗
PubMed2006

Phosphorus(I) iodide: a versatile metathesis reagent for the synthesis of low oxidation state phosphorus compounds.

An improved method for the synthesis of cyclic low oxidation state P cations is presented. The only byproducts of the reaction of phosphorus triiodide with chelating phosphines are readily removed, resulting in an easily accessible P(I) reagent with an anion that can be readily replaced through salt metathesis chemistry. These P(I) salts are surprisingly stable, even in O2 and moisture, and the origin of this unusual stability is elucidated using density functional theory calculations.

Journal Article↗