A high performance thin layer chromatographic (HPTLC) method for the simultaneous quantification of lignocaine hydrochloride (LIG) and phenylephrine hydrochloride (PHE) is described. The mobile phase consisted of ethyl acetate-methanol ammonia (4:1:0.4 v/v/v). The densitometric determination of LIG and PHE was carried out at 262 nm and 291 nm, respectively. The calibration curves of LIG and PHE were linear in the range of 8-18 microg and 4-9 microg, respectively. The method was validated with respect to system precision, method precision, recoveries, intra-day and inter-day variation. The system was applied for the simultaneous determination of LIG and PHE from a new drug delivery system. The results indicate that the method is simple, specific, selective and reliable for simultaneous quantitative determination of LIG and PHE as bulk drug and from formulations.
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http://dx.doi.org/10.1016/s0731-7085(99)00295-2 | DOI Listing |
Biochem Pharmacol
October 2012
Digestive Diseases Branch, NIDDK, National Institutes of Health, Bethesda, MD 20892-1804, USA.
There is increased interest in the Bn-receptor family because they are frequently over/ectopically expressed by tumors and thus useful as targets for imaging or receptor-targeted-cytotoxicity. The synthetic Bn-analog, [D-Tyr(6), β-Ala(11), Phe(13), Nle(14)]Bn(6-14) [Univ.Lig] has the unique property of having high affinity for all three human BNRs (GRPR, NMBR, BRS-3), and thus could be especially useful for this approach.
View Article and Find Full Text PDFPLoS One
December 2010
Centre for Cellular and Molecular Biology, Council of Scientific and Industrial Research, Hyderabad, India.
Background: Many bacterial surface exposed proteins mediate the host-pathogen interaction more effectively in the presence of Ca²+. Leptospiral immunoglobulin-like (Lig) proteins, LigA and LigB, are surface exposed proteins containing Bacterial immunoglobulin like (Big) domains. The function of proteins which contain Big fold is not known.
View Article and Find Full Text PDFBiochim Biophys Acta
December 2004
Dipartimento di Biologia and Laboratorio Interdipartimentale di Microscopia Elettronica, Università Roma Tre, Viale Guglielmo Marconi 446, I-00146 Roma, Italy.
NO-donors block Plasmodium, Trypanosoma, and Leishmania life cycle by inactivating parasite enzymes, e.g., cysteine proteinases.
View Article and Find Full Text PDFEur J Biochem
June 2001
Dipartimento di Biologia, Università 'Roma Tre', Roma, Italy.
Cysteine proteinases are relevant to several aspects of the parasite life cycle and of parasite-host relationships. Here, a quantitative investigation of the effect of temperature and pH on the total substrate inhibition of cruzipain, the major papain-like cysteine proteinase from Trypanosoma cruzi, is reported. Values of the apparent catalytic and inhibition parameters Km, Vmax, Vmax/Km, and K(i) for the cruzipain-catalysed hydrolysis of N-alpha-benzyloxycarbonyl-L-phenylalanyl-L-arginine-(7-amino-4-methylcoumarin) (Z-Phe-Arg-AMC) and azocasein were determined between 10.
View Article and Find Full Text PDFJ Pharm Biomed Anal
May 2000
Department of Chemical Technology, University of Mumbai, Matunga, India.
A high performance thin layer chromatographic (HPTLC) method for the simultaneous quantification of lignocaine hydrochloride (LIG) and phenylephrine hydrochloride (PHE) is described. The mobile phase consisted of ethyl acetate-methanol ammonia (4:1:0.4 v/v/v).
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