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A Kinawi

Publications and source records attributed to A Kinawi.

28 records · Page 2Linked to original sources

[Studies on the interaction of Phenprocoumon with Diazepam and with Nitrazepam (author's transl)].

The influence of Diazepam and Nitrazepam on the anticoagulating activity of Phenprocoumon was studied in rats. It was found that the repeated oral application of Diazepam or Nitrazepam during the treatment with Phenprocoumon did not change the adjusted prothrombin time. The prothrombin time was considerably shortened when the application of Diazepam or Nitrazepam was stopped although Phenprocoumon was still applied. Furthermore, the influence of Chlordiazepoxid, Diazepam and Nitrazepam on the normal prothrombin time was studied. It was found that the treatment with benzodiazepine derivatives had no influence upon the prothrombin time, not only during the treatment, but also after the treatment was stopped.

4-Hydroxycoumarins↗

[The reaction of cyclohexylsulphamic acid (Cyclamate) with nitrous acid in aqueous HCl-solution, isolated human gastric juice and urine (author's transl)].

The pH dependence of the formation and decomposition of the N-nitroso derivative, which is produced by the reaction of cyclohexylsulphamic acid with nitrous acid, was investigated by means of continuous photometric measurement of the changes in absorbance. Reaction at pH 2.45 resulted in an optimal yield of the N-nitroso derivative. The half-life of the decomposition reaction (the reactants cyclohexylsulphamic acid/sodium nitrite being in a molar ratio of 1:1.11) at pH 2.61 was 13.6 min. The N-nitroso derivative showed a relatively high stability at pH 4.5. The reaction in isolated human gastric juice and urine showed the same pH dependency as in aqueous HCl solution.

Cyclamates↗

[Investigation of the interaction of carbamazepine or promazine with bovine serum albumin, using a new dialysis device (author's transl)].

The construction and operation of a new dialysis device are described. The unbound fraction of a drug in a buffered solution of albumin can be determined after 10-15 minutes. The usefullness of this device was demonstrated by the determination of the unbound fraction of Carbamazepine or Promazine in buffered solutions of bovine serum albumin. The results agreed with those obtained by control methods (equilibrium dialysis and gel filtration). Furthermore, the binding of Carbamazepine to bovine serum albumin was characterised by determining the overall binding constant (K1), the apparent binding constant (k+), the number of binding sites per molecule of albumin (n), the free reaction energy deltaFdegrees, and the unbound fraction of the drug.

Binding Sites↗

[Studies on the reactability of chlordiazepoxide to its N-nitrosos derivative in physiological conditions (author's transl)].

It is shown that chlordiazepoxide readily reacts with sodium nitrite in an aqueous HCl solution as well as in human gastric juice to N-nitrosochlordiazepoxide with a high yield (up to 75%). For this reaction the pH optimum has been determined to be 1.4. After oral application of chlordiazepoxide alone or in combination with nitrite to rats, the drug as well as its N-nitroso derivative were recovered from serum and analysed by high-pressure liquid chromatography.

Animals↗

[Determination of 3-(1'-phenylpropyl)-4-hydroxycoumarin by means of high-performance liquid chromatography (HPLC) (author's transl)].

Marcumar [3-(1-phenylpropyl)-4-hydroxycoumarin] was determined by means of high-performance liquid chromatography from serum extracts after the oral application of its sodium salt solution. 4-Hydroxycoumarin was used as the internal standard and rats were used as the test animals. Furthermore mixtures containing anticoagulants and anti-epileptics were also analysed with the help of high-performance liquid chromatography.

4-Hydroxycoumarins↗

[Studies of the interractions of cyclamate with phenprocomon (author's transl)].

The effect of cyclamate on the anticoagulant activity of phenprocoumon was investigated in rats after single oral doses of phenprocoumon, cyclamate, or phenprocoumon/cyclamate. By means of high pressure liquid chromatrography [HPLC] the change of the concentration of phenprocoumon per unit time in sera was determined. The anticoagulant acitivity of phenprocoumon was determined by the extension of the prothromin-time (Quick-test). It was found that cyclamate gives rise to an elevated of phenprocoumon in the blood, and a reduction of the anticoagulanting potency.

4-Hydroxycoumarins↗

[Studies on the interactions of phenprocoumon with chlordiazepoxide in rats (author's transl)].

The influence of Chlordiazepoxide (Librium) on the anticoagulating activity of Phenprocoumon (Marcumar) was investigated in rats. It was found that this psychotropic drug influences neither the anticoagulating activity nor the normal prothrombin-time when it is applied alone or together with Phenprocoumon. However, the prothrombin-time is shortened when Chlordiazepoxide is withdrawn and the feeding of Phenprocoumon is continued.

4-Hydroxycoumarins↗

[Studies on the interactions of chlordiazepoxide, nitrazepam, and diazepam with phenprocoumon (author's transl)].

The interaction of benzodiazepine derivatives with phenprocoumon (Marcumar) was investigated after a single dose of the combination of phenprocoumon/diazepoxide (Librium), phenprocoumon/diazepam (Valium) and phenprocoumon/nitrazepam (Mogadan) had been applied to rats. By means of the high pressure liquid chromatography (HPLC) the change of concentration of these pharmaceutical agents per unit time in serum was determined and related to the corresponding change of prothrombin-time. Hence it can be concluded that the benzodiazepine derivatives influence the distribution of phenprocoumon in the organism.

4-Hydroxycoumarins↗

Progelatinase B forms from human neutrophils. complex formation of monomer/lipocalin with TIMP-1.

The three forms of neutrophil gelatinase B-monomer, homodimer and monomer/lipocalin complex-, were isolated from phorbolester stimulated neutrophil granulocytes by chromatography on gelatin-Sepharose and heparin-Ultrogel. On average, about 50% of the monomer/lipocalin complex was found to be complexed with TIMP-1. After activation with trypsin monomer, homodimer and monomer/lipocalin complex displayed a specific activity of about 2000 mU/mg towards the substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-lle-Ala-Gly-Gln-D-Arg, whereas the monomer/lipocalin/TIMP-1 complex could be activated to a specific activity of only 200 mU/mg. The ternary monomer/lipocalin/TIMP-1 complex behaves like the progelatinase A-TIMP-2 complex and the progelatinase B-TIMP-1 complex in that it is an inhibitor for active metalloproteinases (MMPs) and, after activation, a gelatinase with a pronouncedly reduced activity. When the monomer/lipocalin/TIMP-1 complex inhibits an MMP, a quaternary complex monomer/lipocalin/TIMP-1/MMP is generated which after activation shows a sixfold higher proteolytic activity than the active ternary complex.

Carrier Proteins↗