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3. Capillary electrophoresis device with double UV detection and its application to the determination of effective mobilities of peptides

Author

Štěpánek Jiří, Prusík Zdeněk, Petr Mudra, and Kasicka Vaclav

Subjects
Electrophoresis, Chromatography, Uv detector, Chemistry, Capillary action, Instrumentation, Organic Chemistry, Molecular Sequence Data, Analytical chemistry, Temperature, General Medicine, Biochemistry, Analytical Chemistry, Capillary electrophoresis, Optical path, Diglycine, Spectrophotometry, Ultraviolet, Amino Acid Sequence, Uv detection, Peptides
Abstract

A new experimental device for high-performance capillary electrophoresis (HPCE) with a double UV detection system and with thermostating of the whole separation compartment was developed. UV detection is doubled by producing two apertures placed symmetrically close to the axis of the optical path of the single-beam UV detector and by the adjustment of the capillary loop on these two apertures. The double-detection system allows exact measurements of electrophoretic and electroosmotic flow velocities. A procedure for the determination of effective mobilities from the data obtained by the double UV detection system was developed and applied to determine the effective mobilities of synthetic peptides (diglycine, triglycine, growth hormone releasing peptide and its derivatives and fragments). The measurements are performed at constant temperature (25 degrees C) and low input power at which temperature increase in the capillary can be neglected and temperature corrections of temperature-dependent magnitudes need not be included in the calculations.

Published
1995

16. Porcine Luteinizing Hormone and its Subunits.

Author

Hennen, Georges, Prusík, Zdeněk, and Maghuin-Rogister, Guy

Subjects
*LUTEINIZING hormone, *CHROMATOGRAPHIC analysis, *IMMUNOLOGY, *LYSINE, *ELECTROPHORESIS, *AMINO acids
Abstract

A new method is described for the isolation of the subunits of porcine luteinizing hormone which have not been characterized before. By chromatography on SE-Sephadex C-25 in 8 M urea, the two subunits LHα and β were obtained in good yield and without apparent cross contamination. The physicochemical and immunological properties of these subunits were studied. Unlike the bovine or ovine LHβ subunits described earlier, porcine LHβ subunit does not contain lysine. Porcine LHα subunit is electrophoretically heterogeneous and two components represented by two homogeneous electrophoretical zones were isolated and characterized. The amino acid composition of these components is very similar; they differ, however, slightly in peptide maps of their tryptic digests. Whole LHα subunit was submitted to specific cleavage at methionine residues by cyanogen bromide and a homogeneous peptide not containing homoserine was isolated. The latter represents most probably the C-terminal fragment of LHα subunit. Its partial amino-acid sequence and composition is: Gly-Asn-Ala-Arg-Val-Glu-(His3,Lys,CM-Cys3-4,Asp,Thr2,Ser,Glu,Tyr2)-Ser. The fragment contains 34% of sugar (by weight). In view of the similarity in peptide maps and the unambiguous sequence described above, the primary structure of the different components of LHα subunit must be very similar. [ABSTRACT FROM AUTHOR]

Published
1971
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21. Synthesis and properties of the Nα-glycyl-glycyl-glycyl-8-lysine-vasopressin and its des-glycinamide derivative

Author

Procházka, Zdenko, primary, Krejčí, Ivan, additional, Kupková, Běla, additional, Slaninová, Jiřina, additional, Bojanovska, Vera, additional, Prusík, Zdeněk, additional, Vosekalna, Ilse A., additional, Maloň, Petr, additional, Barth, Tomislav, additional, Frič, Ivo, additional, Bláha, Karel, additional, and Jošt, Karel, additional

Published
1978
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