Biomedical subjects

Y Boulanger

Publications and source records attributed to Y Boulanger.

112 records · Page 7Linked to original sources

PubMedDate not supplied

Purification and characterization of bolaffinine, a toxic protein from Boletus affinis Peck (Boletaceae).

A toxic protein of Mr 22,000, called bolaffinine, has been purified from the mushroom, Boletus affinis Peck (Boletaceae), with a 0.65% yield using a procedure involving four steps: ammonium sulfate precipitation, two chromatographies on ion-exchange columns and gel filtration on Sephadex G-75. It is thermolabile and can be inactivated by organic solvents. Its isoelectric point lies between pH 9 and 10. It contains 234 amino acids, no free SH groups and one disulfide bridge as evidenced by reactions with 5-5'-dithiobis-nitrobenzoate (DTNB) and 2-mercaptoethanol. When injected into mice, it provokes the death of animals within 16-24 h. The 24 h LD50 is 61 mg/kg of body weight. Bolaffinine inhibits protein synthesis in hepatoma tissue culture and in a rabbit reticulocyte lysate.

Amino Acids↗

PubMedDate not supplied

Purification and characterization of a toxin inhibiting protein synthesis from Croton mongue, a Madagascar Euphorbiaceae.

Monguine, a thermostable toxic protein was extracted from the seeds of Croton mongue (Euphorbiaceae) and purified by ion-exchange chromatography on DEAE-cellulose and gel filtration on Sephadex G-25 and G-15. Polyacrylamide gel electrophoresis of purified monguine in the presence of sodium dodecyl sulfate and after treatment with 2-mercaptoethanol showed one band corresponding to a molecular weight of 9000. The same molecular weight was determined by analytical centrifugation. Amino acid analysis revealed a high content in both aspartic and glutamic acids (or the corresponding amides). The LD50 (24 h) is 12 mg/kg of mouse body weight. Monguine inhibits protein synthesis in hepatoma tissue culture cells and globin synthesis in a rabbit reticulocyte lysate.

Amino Acids↗

PubMedDate not supplied

Heterogeneous metabolism and toxicity of 4-pentenoate along the dog nephron.

4-Pentenoate (4P) is a short-chain fatty acid which causes a complete renal Fanconi syndrome. We have examined the mechanism of 4P toxicity along the nephron after a prolonged (30 min) exposition of isolated renal tubular segments to this agent. In proximal tubules, 4P inhibited the activity of alpha-ketoglutarate dehydrogenase, pyruvate dehydrogenase, and beta-oxidation, but not in thick ascending limb or inner medullary collecting duct tubules in suspension. These proximal effects were accompanied by a marked oxidation of the proximal redox state, with a fall in the tissue respiration and a low content of ATP. The acetyl-CoA content of proximal tubules was simultaneously reduced. Butyrate, acetate, hexanoate or octanoate did not exert these effects. In proximal tubules the metabolism of 4P led to the tissue accumulation of 3-keto-4-pentenoyl-CoA, a known unspecific inhibitor of metabolic oxidation. This metabolite was not detectable in thick ascending limbs which metabolized 4P rapidly. No metabolism of 4P was noted in collecting ducts. We conclude that beta-oxidation probably differs in proximal and thick ascending limb tubules, allowing 4P metabolism to exert a specific toxicity in proximal tubules. A selective proximal defect in energy metabolism probably explains the Fanconi syndrome observed with exposition to 4P.

Amino Acids↗

PubMedDate not supplied

Structure of human calcitonin gene-related peptide (hCGRP) and of its antagonist hCGRP 8-37 as determined by NMR and molecular modeling.

The solution structures of human calcitonin gene-related peptide (hCGRP, 37 residues) and of its antagonistic fragment hCGRP 8-37 have been determined by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy and molecular modeling. Analysis of the double quantum filtered correlation spectroscopy, total correlation spectroscopy and nuclear Overhauser enhancement spectroscopy spectra led to a complete assignment and to the identification of more than 350 intra- and interresidue connectivities for each peptide. Molecular models were calculated by molecular dynamics and energy minimization using distance constraints. The structure of hCGRP is characterized by a rigid N-terminal disulfide-bonded loop followed by helix segments (Val8-Leu16), a gamma-turn (Ser19-Gly21) and several local hydrogen-bonded patterns. The structure of hCGRP 8-37 is less defined than the structure of hCGRP and no helix structure is present. Molecular models of both peptides are consistent with the NH temperature coefficients and secondary chemical shifts of the alpha-protons. Hydrogen bonding with the disulfide-bonded ring appears to be critical for helix formation, both structural elements being essential for agonistic activity.

Amino Acid Sequence↗