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Biomedical subjects

A Kinawi

Publications and source records attributed to A Kinawi.

At least 19 recordsLinked to original sources
PubMed1996

Further development of flow-through electrophoresis.

Recent improvements in the field of flow-through-electrophoresis are presented. These improvements make it possible to run flow through electrophoresis with the same precision, but more economically and more easily than the formerly described apparatus. This was achieved by limiting the original system to slab gels only. This leads to a considerable reduction in the size of the apparatus and to simplification of its handling. Although the gel width is reduced to 10 mm, the apparatus is suitable for the analysis of mg as well as microgram quantities. The usefulness of this method is demonstrated by the analysis of samples obtained during the isolation and purification of collagen type II, and by the analysis of insulin samples and other substances. The procedure is also suitable for SDS-electrophoresis under flow-through conditions, enabling a simple and fast separation of proteins and determination of their molecular masses.

Bromphenol Blue↗
PubMed1989

[Binding of racemic indoprofen and its enantiomers to human serum albumin].

Binding of Racemic Indoprofen and its Enantiomers to Human Serum Albumin. The binding to 2% and 4% human serum albumin (HSA) of (+/-)-indoprofen, (-)-indoprofen, and (+)-indoprofen was examined applying a modified ultrafiltration process. The binding properties to HSA were characterized by determining the unbound portions of the drug (a), the overall binding constants (K1), the free reaction energy (delta F degrees), the apparent binding constants (k*), and slope (m). The following results were obtained: 1. Racemic indoprofen and its enantiomers show a high affinity to human serum albumin (a = 1-2%). 2. At higher HSA concentrations the free portion (a) diminishes. 3. The affinity to HSA is reduced in the order of levo-indoprofen racemic indoprofen, and dex-indoprofen.

Humans↗
PubMed1988

[The binding of oxicam derivatives to human serum albumin].

The binding characteristics of several oxicam derivatives (tenoxicam, 4-hydroxy-2-methyl-N-phenyl-2H-1,2-benzothiazixine-3- carboxamide-1,1-dioxide (CP 14,304), 4-hydroxy-2-methyl-N-2-(3-methyl)-pyridyl-2H-1,2-benzothiazixine-3 -carboxamide- 1,1-dioxide (CP 16,460), piroxicam, meloxicam [corrected], isoxicam, 5-hydroxy-piroxicam) to 2% and 4% human serum albumin (HSA) were determined using a modified ultrafiltration process. The binding properties to HSA were characterized by determining the overall binding constant, the apparent binding constant, the slope, the free reaction energy, and the unbound portion of the drug. The following results were obtained: 1. These oxicam derivatives show a high affinity to HSA. The unbound fraction amounts to 1-3%. 2. The affinity of the compounds to HSA decreases in the order mentioned above. 3. Doubling of the HSA concentration reduces the unbound fraction, to the half, with piroxicam being the only exception.

Anti-Inflammatory Agents, Non-Steroidal↗
PubMed1985

[Flow-through electrophoresis].

The construction, the main technical details and the handling of a new electrophoretic apparatus1) are described. This system can be used for flow-through electrophoresis, as well as all slab or tube gel techniques. The suitability of the apparatus is demonstrated by the electrophoretic analysis of different samples by flow-through electrophoresis.

Buffers↗
PubMed1984

[Determination of the binding of 3,5-bis(acetamido)-2,4,6-triiodobenzoic acid and some of its salts to human serum albumin using the ultrafiltration flat chamber method].

Using the ultrafiltration flat chamber method the binding of N-methylglucamine, meglumine amido trizoate, lysine amido trizoate, diatrizoic acid and L-lysine to human serum albumin (HSA) was investigated. It was demonstrated that the affinity to HSA decreases in the above mentioned order. Binding was characterised by determination of K1 (total binding constant), k+ (apparent binding constant), n (number of binding sites per molecule of albumin) and delta F degrees (free reaction energy).

Chemical Phenomena↗
PubMed1979

[Determination of drug-albumin binding in buffered bovine serum albumin solutions applying a modified ultrafiltration process (author's transl)].

The construction of two ultrafiltration devices which, under application of high-pressure liquid chromatographic (HPLC) technique, allow the determination of unbound portions of drugs in albumin solutions is described. The usefulness of this method and its advantages compared with prevailing methods are demonstrated by means of determination of the unbound portion of carbamazepine, chlorpromazine, phenobarbital and phenprocoumon in buffered bovine serum albumin solutions (4%). The binding of each drug to albumin was characterised by determining the overall binding constant (K1), the apparent binding constant (k+), the free reaction energy (delta F0), the number of binding sites per albumin molecule (n), the rate of taking up of drug by albumin (V) and the unbound portions of the drug (alpha).

Animals↗
PubMed1978

[Reaction kinetic studies on the formation of n-nitrosoephedrine in vitro and in vivo (author's transl)].

N-Nitrosoephedrine was synthesized at a high yield (greater than 90%). The influence of pH on the reaction process (ephedrine sulfate + nitrous acid in hydrochloric acid) was investigated and the pH-optimum determined. Furthermore the influence of coffee, ascorbic acid, citric acid, cyclamate/saccharin (10:1), smoke condensate of cigarettes, glucose and ethanol on the reaction process was also determined. The tests with animals (rats) showed that N-nitrosoephedrine could be detected in serum after the oral application of ephedrine sulfate and sodium nitrite.

Animals↗