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Sodium alginate and pectin estimation in raft forming pharmaceuticals by high performance liquid chromatography method

100%

Hanif M. , Shah S. , Rasool N. , Abbas G. , Saadullah M. , Khan S. M. , Ahmed M. M. , Abbas N. , Ashfaq M. , Iqbal O.

Acta Chromatographica

2021

tom Vol. 33, no. 2

127--133

The high performance liquid chromatographic (HPLC) method was developed for the combined estimation of sodium alginate and pectin in raft forming pharmaceuticals on C18 column ZORBAX ODS (1.5 cm × 4.6 mm, 5 μm) with UV detection at 378 nm. The assay condition comprised of phosphate buffer pH 7.4 and methanol 60:40% v/v at a flow rate of 1.25 mL/min. The separation of sodium alginate and pectin with good resolution and a retention time less than 8 min was attained. The method was linear over a range of 200–800 μg/mL of sodium alginate and pectin. The regression values obtained from linearity curve of sodium alginate and pectin were 0.9993 and 0.9991, respectively. The retention time of sodium alginate and pectin was 3.931 and 7.470 min, respectively. The percent recovery of sodium alginate and pectin ranged from 94.2–98.5% and 92.1–98.4% respectively. The limit of detection (LOD) and limit of quantification (LOQ) of sodium alginate were found to be 2.443 and 3.129 μg/mL and the LOD and LOQ of pectin were 3.126 and 3.785 μg/mL, respectively. The resolution of sodium alginate and pectin was found in the range of 1.03–1.89 and 1.10–1.91, respectively. This method has been successfully applied to analyze the concentrations of sodium alginate and pectin in raft forming drug delivery systems.

Influence of the Static Loading of a Raft Unconnected to a Pile on the Pile Displacements Tested in Field Conditions

75%

Sedin V. , Bikus K. , Kovba V. , Kononov D. , Zahilskyi V.

Civil and Environmental Engineering Reports

2019

tom Vol. 29, no. 2

22--30

We present the results of a static pile-raft interaction test in field conditions. The pile and the raft were unconnected. The static loading on the raft affected the displacements of the pile due to the skin friction. The displacements were also observed for another pile, placed at the 3-metre distance.

Rafts - the current picture

63%

Grzybek M. , Kozubek A. , Dubielecka P. , Sikorski A. F.

Folia Histochemica et Cytobiologica

2005

tom 43

nr 1

Estonia - a land of big boulders and rafts

63%

Raukas A.

Quaestiones Geographicae. Zeszyt Specjalny

1995

tom 04

Smooth muscle actomyosin promotes Ca2plus - dependent interactions between annexin VI and detergent-insoluble glycosphingolipid-enriched membrane domains

51%

Babiychuk V. S. , Draeger A. , Babiychuk E. B.

Acta Biochimica Polonica

2000

tom 47

nr 3

The mechanical link coupling cytoskeletal and contractile proteins to the sarcolemma of smooth muscle cells is essential for transmitting tension from the cell's interior to exterior. In addition to the well-characterized actin-integrin associations present in adhaerens junctions, our recent work has postulated the existence of a reversible annexin-dependent membrane-cytoskeleton complex, forged in response to a rise in intracellular Ca2+ concentration following smooth muscle cell stimulation (Babiychuk et al., J. Biol Chem. 1999, 274, 35191-35195). Detailed biochemical characterization of the interactions responsible for the formation of this complex revealed that annexins II and VI interact with actomyosin, or detergent-insoluble glycosphingolipid-enriched membrane domains (rafts) purified from smooth muscle, in a concentration- and Ca2+-dependent manner. Annexin II interacted with lipid rafts with high Ca2+-sensitivity, while for annexin VI this interaction required non-physiologically high concentrations of free Ca2+. However, the Ca2+-sensitivity of the latter interaction strongly increased in the presence of purified smooth muscle actomyosin. The detailed biochemical analysis of the interactions occurring between annexin II, annexin VI, actomyosin and rafts suggests that annexins regulate sarcolemmal organization during smooth muscle cell contraction.