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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Qualitative and quantitative reversed-phase high performance liquid chromatographic analysis of glycoprotein hormones in the presence of a large excess of human serum albumin

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Author(s):
Almeida, B. E. [1] ; Oliveira, J. E. [1] ; Damiani, R. [1] ; Dalmora, S. L. [2] ; Bartolini, P. [1] ; Ribela, M. T. C. P. [1]
Total Authors: 6
Affiliation:
[1] IPEN CNEN, Dept Biotechnol, BR-05508900 Sao Paulo - Brazil
[2] Univ Fed Santa Maria, Dept Ind Pharm, BR-97119900 Santa Maria, RS - Brazil
Total Affiliations: 2
Document type: Journal article
Source: Journal of Pharmaceutical and Biomedical Analysis; v. 63, p. 160-164, APR 7 2012.
Web of Science Citations: 2
Abstract

The present work describes reversed-phase high performance liquid chromatographic methodologies (RP-HPLC) for the qualitative and quantitative analysis of the human glycoprotein hormones thyrotropin (hTSH), follitropin (hFSH), choriogonadotropin (hCG) and lutropin (hLH) in the presence of a large excess (up to 250:1) of human serum albumin (HSA). Chromatographic profiles with a good separation between the hormone and HSA were obtained by using a C4 column and specific gradient elution conditions for each hormone. Parameters such as resolution factor, tailing factor and relative retention time, were determined, and are useful for the evaluation of the quality of the separation obtained between the active pharmaceutical ingredient and the excipient present in the final formulation. The potential of each method for quantification of both HSA and the hormone was also demonstrated. Besides furnishing chromatographic quantifications that can substitute for in vivo bioassays and animal use, the chromatograms also provide a direct panorama of the quality and heterogeneity of the protein of interest. (C) 2012 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 11/07289-0 - Synthesis and characterization of different glycoforms of recombinant human thyrotropin (rhTSH) pharmacologically actives
Grantee:Maria Teresa de Carvalho Pinto Ribela
Support Opportunities: Regular Research Grants