muramidase and pyranine

muramidase has been researched along with pyranine* in 2 studies

Other Studies

2 other study(ies) available for muramidase and pyranine

ArticleYear
Drug release from lipid-based implants: elucidation of the underlying mass transport mechanisms.
    International journal of pharmaceutics, 2006, May-18, Volume: 314, Issue:2

    The aim of this study was to better understand the mass transport mechanisms involved in the control of drug release from lipid-based implants. Different types of triglyceride-based cylinders were prepared by compression. Glycerol-trilaurate, -trimyristate, -tripalmitate and -tristearate were used as model lipids, lysozyme and pyranine as model drugs. The effects of several formulation and processing parameters on the resulting drug release kinetics in phosphate buffer pH 7.4 were studied and the obtained results analyzed using Fick's second law of diffusion. Interestingly, lysozyme release from implants prepared by compression of a lyophilized emulsion (containing dissolved drug and lipid) was found to be purely diffusion-controlled, irrespective of the type of triglyceride. In contrast, the dominating release mechanism depended on the type of lipid in the case of pyranine-loaded implants prepared by compression of a lyophilized lipid-drug solution: with glycerol-trilaurate and -tristearate the systems were found to be purely diffusion-controlled, whereas also other mass transport phenomena are of importance in glycerol-trimyristate and -tripalmitate-based devices. Similarly, changes in the size of the compressed lipid-drug particles, drug loading and compression force significantly affected the underlying release mechanisms. The addition of a drug-free, poly(lactic-co-glycolic acid) (PLGA)-based coating around the implants delayed the onset of pyranine release for about 20 days. Interestingly, the subsequent drug release was purely diffusion-controlled, irrespective of the type of triglyceride. Also the addition of different amounts (and particle size fractions) of saccharose to pyranine-loaded implants led to purely diffusion-controlled drug release.

    Topics: Arylsulfonates; Biological Transport; Chemistry, Pharmaceutical; Diffusion; Drug Carriers; Drug Implants; Kinetics; Lactic Acid; Lipids; Models, Chemical; Muramidase; Particle Size; Polyglycolic Acid; Polylactic Acid-Polyglycolic Acid Copolymer; Polymers; Porosity; Solubility; Sucrose; Technology, Pharmaceutical; Triglycerides

2006
Proton transfer dynamics in the nonhomogeneous electric field of a protein.
    Biophysical journal, 1991, Volume: 59, Issue:1

    By adsorption of pyranine (8 hydroxypyrene 1, 3, 6 trisulfonate) to lysozyme we create on the positively charged protein a fluorophoric site with a total charge of -3. Photo dissociation of the dye's hydroxyl proton changes its absorption and fluorescence spectrum, permitting a continuous monitoring of the reprotonation dynamics. Absorbance measurements in the microsecond time scale monitor how the bulk protons penetrate the Coulomb cage of the bound dye. Time-resolved fluorescence monitors how the proton is escaping out of the Coulomb cage of the bound dye. These probe reactions were studied with a series of dye-enzyme complexes where the number of free carboxylate was reduced by amidation, increasing the total charge of the complex from +5 to +12.6. The time-resolved measurements demonstrate the complexity of the electric field in the immediate vicinity of the dye. It is consistent with a negative potential wall (of the anion) surrounded by a positive potential wall of proteinaceous moieties.

    Topics: Adsorption; Arylsulfonates; Binding Sites; Electrochemistry; Kinetics; Muramidase; Protein Conformation; Protons; Time Factors

1991