pH Effects (ph + effects)

Distribution by Scientific Domains


Selected Abstracts


Determination of physicochemical properties of tetrabromobisphenol A

ENVIRONMENTAL TOXICOLOGY & CHEMISTRY, Issue 12 2008
Hidetoshi Kuramochi
Abstract Aqueous solubility (Sw), 1-octanol/water partition coefficient (KOW), and vapor pressure of the nonionic form of 2,2,,6,6,-tetrabromo-4,4,-isopropylidenediphenol (tetrabromobisphenol A or TBBP-A) were measured. From this, enthalpies of solution and vaporization were estimated. Furthermore, enthalpy of fusion and melting point were measured to estimate subcooled liquid vapor pressure, the infinite dilution activity coefficient, and Henry's law constant. Since TBBP-A is expected to exit in both ionic and nonionic forms at near neutral pH, pH effects on physicochemical properties were also examined. Because of the ionization of TBBP-A, Sw increased by five orders of magnitude, while KOW decreased by eight orders of magnitude. Furthermore, an analytical model based on mass balance and dissociation of TBBP-A was applied to represent the pH dependence. [source]


Titration and Assignment of Residues that Regulate the Enantioselectivity of Phenylacetone Monooxygenase

ADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 8-9 2007
Francesca Zambianchi
Abstract Phenylacetone monooxygense (PAMO) from Thermobifida fusca was employed for the asymmetric oxidation of thioanisole (sulfooxidation) and of racemic 2-phenylpropionaldehyde (Baeyer,Villiger oxidation). A pH dependence of enantioselectivity was observed in both cases. Two different residues, with pKa values of 7.8±0.2 and 9.2±0.2, appeared to be responsible for the pH effects on PAMO enantioselectivity. The protonation of Arg337 and the FAD:C4a-hydroperoxide/FAD:C4a-peroxide equilibrium were identified as the major factors responsible for the fine-tuning of PAMO enantioselectivity in Baeyer,Villiger oxidation and sulfooxidation, respectively. [source]


Human laminin-332 degradation by Candida proteinases

JOURNAL OF ORAL PATHOLOGY & MEDICINE, Issue 6 2008
P. Pärnänen
Background:, Human laminin-332 (Lm-332) degradation by 12 Candida strains and effects of synthetic proteinase inhibitors [Ilomastat (ILM), EDTA, chemically modified tetracycline-3(CMT-3), CMT-308, synthetic peptide CTT-2, and Pefabloc] were studied. Materials and methods:, Laminin-332 was incubated with sonicated cell fractions and 10 times concentrated cell-free fractions of reference and clinical strains of C. albicans, C. dubliniensis, C. guilliermondii, C. glabrata, C. krusei, and C. tropicalis. Proteolysis, pH effects, and inhibitors were analyzed by fluorography and zymography. Results:, Cell fractions of all species except C. guilliermondii and cell-free fractions of C. albicans, and C. dubliniensis showed 20,70 kDa gelatinases at pH 5.0 and 6.0. At pH 7.6, C. glabrata, C. krusei, and C. tropicalis cell fractions and C. tropicalis cell-free fractions showed 55,70 kDa gelatinases. CMT-3, CMT-308, and CTT-2 inhibited Candida gelatinases slightly better than Pefabloc, ILM, and EDTA. No Candida fractions degraded Lm-332 at pH 7.6, but at pH 5.0, 100 kDa bands were generated by cell fractions of C. dubliniensis and C. tropicalis; C. albicans and C. glabrata clinical strains; and C. guilliermondii reference strain. C. krusei reference strain yielded three 100,130 kDa bands. C. albicans, C. dubliniensis, and C. tropicalis reference and clinical strain's cell-free fractions generated 100 kDa band. Conclusions:, Laminin-332 degradation is pH-dependent and differences exist between studied Candida strains. Lm-332 degradation can exert functional disturbances on basement membrane integrity, possibly aiding Candida cell invasion into tissues. Certain synthetic matrix metalloproteinase inhibitors (CMTs, CTT) can inhibit Candida proteinases and may be therapeutically useful in future. [source]


Mechanism of lidocaine release from carbomer,lidocaine hydrogels

JOURNAL OF PHARMACEUTICAL SCIENCES, Issue 1 2002
Alvaro Jimenez-Kairuz
Abstract Rheology, acid-base behavior, and kinetics of lidocaine release of carbomer,lidocaine (CL) hydrogels are reported. A series of (CL)x (x,=,mol% of L,=,25, 50, 75, 100) that covers a pH range between 5.33 and 7.96 was used. Concentrations of ion pair ([R-COO,LH+]) and free species (L) and (LH+) were determined by the selective extraction of (L) with cyclohexane (CH) together with pH measurements, i.e., CH in a ratio CH/hydrogel 2:1 extracted 48% of the whole concentration of lidocaine [LT] of a (CL)100, {[LT],=,([R-COO,LH+]),+,(L),+,(LH+)}. The remaining species in the aqueous phase were distributed as: (L) 3.82%, (LH+) 14.5%, and [R-COO, LH+] 81.7%. Rheology and pH as a function of (CL) concentration are also reported. Delivery rates of free base L were measured in a Franz-type bicompartmental device using water and NaCl 0.9% solution as receptor media. (CL) hydrogels behave as a reservoir that releases the drug at a slow rate. pH effects on rate suggest that, under the main conditions assayed, dissociation of [R-COO,LH+] is the slow step that controls releasing rates. Accordingly, release rate was increased upon addition of a second counterion (i.e., Na+), or through the diffusion of neutral salts such as NaCl, into the matrix of the gel. © 2002 Wiley-Liss, Inc. and the American Pharmaceutical Association J Pharm Sci 91:267,272, 2002 [source]