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PubMed1982

The elongation factor 1 from wheat germ: structural and functional properties.

Three forms of elongation factor 1 (EF1A, EF1B and EF1C) were isolated from wheat germ; the preparation obtained by successive chromatography on DEAE-Sephadex A-50, hydroxylapatite and Sephadex G-200 showed about 90% purity. The molecular masses of these forms were about: 61 000, 48 000 and 12 500, respectively. EF1A was the only form which formed the ternary complex GTP-EF1-AA-tRNA and was the most active in binding of Phe-tRNA to the poly-U programmed ribosomes. Based on the data of amino acid analysis, N-terminal amino acid determination and previously described proteolysis (Pulikowska et al., Biochem. Biophys. Res. Commun., 1979, 91, 1011-1017), it is assumed that EF1C is a basic structural subunit of elongation factor EF1 from wheat germ, but only EF1A shows the conformation-dependent full biological activity.

Amino Acids↗
PubMed1976

Effect of glycodihydrofuisidate on sulfobromophthalein transport maximum in the hamster.

The effect on sulfobromophathalein transport maximum (Tm) and biliary lipid secretion of sodium glyco-24,25-dihydrofusicate, a micelle-forming compound secreted into bile, has been studied in the hamster and compared to that of a physiological bile salt, sodium taurocholate. Biliary phospholipid and cholesterol secretion increased both during glycodihydrofusidate and taurocholate administration, an observation which suggest that both compounds increased th biliary secretion of micelle-forming compounds. In contrast, only taurocholate increased sulfobromophthalein Tm into bile, while glycodihydrofusidate administration decreased it. This observation suggests that the increase in sulfobromophthalein Tm observed during taurocholate administration is not the result of micellar sequestration. It could rather be the consequence of a specific effect of bile salts on the dye transport system.

Animals↗
PubMed1975

Surface and solution properties of steroid antibiotics: 3-acetoxylfusidic acid, cephalosporin P1 and helvolic acid.

The colloid/chemical properties of the fusidane antibiotics, 3-acetoxylfusidic acid, cephalosporin P1, and helvolic acid, and their sodium salts, were investigated. The sodium salts of 3-acetoxylfusidic acid and cephalosporin P1 were found to be detergent-like molecules with micellar properties comparable to the parent compound sodium fusidate and the bile salt sodium cholate. Critical micellar temperatures (cmt) were less than 0 degrees C except for sodium helvolate which being sparingly soluble did not form micelles between 0 and 50 degrees C. Potentiometric titrations of dilute solutions gave apparent pK values (5.2-6.5) in the range expected for carboxylated steroid detergents. The apparent pK values increased significantly once the detergent concentration exceeded the critical micellar concentration (cmc). Micellar properties were determined by surface tension, titration with a water-soluble dye (Rhodamine 6G), light scattering, and solubilization of lecithin and cholesterol. Cmc's, in the range of 1.5 to 5.6 mM, were found which varied slightly depending on the method employed and in all cases fell slightly in the presence of added NaCl. The number of monomers per micelle (aggregation number) in concentrations well above the cmc was extrapolated from Debye light scattering plots in 0.15 M NaCl. The values varied from 6 for fusidate to 14 for 3-acetoxylfusidate with sodium cephalosporin P1 having an intermediate value. Each detergent readily solubilized the phospholipid lecithin.

Cephalosporins↗
PubMed2006

[Impetigo].

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Administration, Oral↗
PubMed1973

Mechanism of puromycin action: fate of ribosomes after release of nascent protein chains from polysomes.

The exchange of ribosomal subunits during the release of growing polypeptide chains by puromycin has been investigated in a bacterial cell-free system engaged in protein synthesis. The addition of spermidine, used as a stabilizing agent of 70S monomers, caused a strong inhibition of the subunit exchange. This result led us to conclude that upon premature release of unfinished protein chains by the antibiotic, the ribosomes fall off mRNA as 70S particles. This behavior is different from that occurring during physiological termination of translation, where the ribosomes detach in a dissociated form. Some implications of the postulated mechanism are also discussed.

Amino Acids↗
PubMed1990

The effects of permeation enhancers on the surface morphology of the rat nasal mucosa: a scanning electron microscopy study.

A rat model has been developed to compare relative morphological changes in the nasal mucosa after exposure to potential membrane permeation enhancers. Scanning electron microscopy was used to characterize gross structural and specific cellular changes following exposure. Micrographs of the rat nasal mucosa were scored in four categories: (1) mucosal surface integrity, (2) ciliary morphology, (3) mucus/extracellular debris, and (4) presence of red blood cells. The order of increasing morphological damage resulting from a 5-min exposure to each surfactant was 0.5% Solulan C-24 congruent to 0.5% Solulan C-24/0.5% sodium tauro-24,25-dihydrofusidate (STDHF) less than 0.5% STDHF less than 1.0% STDHF much less than 1.0% Laureth-9 less than 1.0% sodium taurodeoxycholate congruent to 1.0% sodium deoxycholate. The changes observed in the mucosal morphology after exposure to the various surfactants are in general agreement with data in the literature. This model is able to compare rapidly the relative morphological effects on the mucosal membrane of different nasal formulations.

Animals↗
PubMed1997

Ribosomes and ribosomal RNA as chaperones for folding of proteins.

BACKGROUND: Provocative recent reports indicate that the large subunits of either prokaryotic or eukaryotic ribosomes have the capacity to promote refolding of denatured enzymes. RESULTS: Salt-washed Escherichia coli ribosomes are shown to promote refolding of denatured rhodanese. The ability of the ribosomes to carry out renaturation is a property of the 50S ribosomal subunit, specifically the 23S rRNA. Refolding and release of enzymatically active rhodanese leaves the ribosomes in an inactive state or conformation for subsequent rounds refolding. Inactive ribosomes can be activated by elongation factor G (EF-G) plus GTP or by cleavage of their 23S rRNA by alpha-sarcin. Activation by either mechanism is strongly inhibited by the EF-G.GDP.fusidic acid complex. CONCLUSIONS: Large subunits of E. coli ribosomes, specifically 23S rRNA, have the capacity to mediate refolding of denatured rhodanese. Refolding activity is related to the state or conformation of ribosomes that is promoted by EF-G. Activation by either mechanism is strongly inhibited by the EF-G.GDP.fusidic acid complex.

Endoribonucleases↗