[Extractive spectrophotometric determination of isopropamide iodide in its pharmaceutical formulations using bromophenol blue, eosine Y and amido black]

We developed simple, rapid, accurate, precise and sensitive spectrophotometric methods for the determination of ISPI in tables. The proposed methods are based on the formation of ion-pair complexes between the examined drug with BPB, AB in alkaline buffer at pH [9.0-9.5] and EO in buffer at pH=6.5, the complexes were extractable with dichloromethane which can be measured at the optimum lambda [max]. beer's law is obeyed in the concentration ranges a 0.96-14.4 micro g.ml[-1], 0.481-7.213 micro g.ml[-1] and 0.962-28.85 micro g.ml[-1] for the complexes ISPI-BPB, EO-ISPI and AB-ISPI respectively. The proposed methods were directly and easily applied to ISPI pharmaceutical preparations with accuracy, with results from recovery experiments ranging between 99.22 and 100.10% for BPB, 98.55 and 102.29% for EO and 98.75 and 101.93% for AB methods. The low relative standard deviation values indicate good precision and high recovery values indicate accuracy of the proposed methods. Therefore the proposed methods have been successfully applied to the determination of drug in commercial tablets

Coomassie brilliant blue R-250 as a highly sensitive pre-stain for immediate visualization of human serum proteins on polyacrylamide gel disc electrophoresis and raising monospecific antibodies.

We hereby describe electrophoretic analysis of normal human serum pre-stained with Coomassie Brilliant Blue R-250 (CBB). The proposed method was optimized by studying as many as 450 disc electrophoretic separations and 30 variables. The method when compared with the post-electrophoretic staining by Amido Black (AB) revealed that the pre-stained discs were intensely well defined and resolved within 2 hours with a transparent gel. Gels stained with AB, despite a prolonged destaining, showed a residual dye retention making identification of the faint components difficult. Protein eluted from the CBB pre-stained gels retained its purity and immunoreactivity and conjugates of the two prototype proteins namely the albumin and the transferrin produced high-titre monospecific antisera in immunized rabbits.