PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
Tytuł artykułu

The chromatographic behavior of wild type and pegylated lysozyme on reversed phase-high performance liquid chromatoraphy media

Wybrane pełne teksty z tego czasopisma
Identyfikatory
Warianty tytułu
Konferencja
Międzynarodowa Konferencja Młodych Naukowców "Środowisko, Rozwój, Inżynieria, Modelowanie" (5 ; 2004 ; Kraków)
Języki publikacji
EN
Abstrakty
EN
The chromatographic behavior of wild type lysozyme and PEGylated lysozyme on silica-based C4 and C18 reversed phase media using and HPLC system was studied. We studied the effects of medias. alkyl chain length on wild type and modified lysozyme. The impact of a covalently bonded PEG chain on the protein.s retention behavior was examined. Using two different reversed phase media we did not observe different elution profiles; adsorption is not influenced by medias. alkyl chain length. According to prior work, the strongly retained wild type lysozyme was structurally perturbed due to adsorption. The elution profile of PEGylated lysozyme showed an even much stronger retained peak fraction, which indicates that PEG has stronger interactions with the hydrophobic stationary phase.
Rocznik
Strony
77--85
Opis fizyczny
Bibliogr. 11 poz., wykr.
Twórcy
autor
  • Fachhochschule Münster, Germany
  • Fachhochschule Münster, Germany
autor
  • Fachhochschule Münster, Germany
Bibliografia
  • [1] De Collongue-Poyet B., Vidal-Madja C., Sebille B., Unger K.K., Study of conformational effects of recombinant interferon gamma adsorbed on a non-porous, Journal of Chromatography, B 664, 1995, 155-161.
  • [2] Balasubramaniam A., Knittel J.J., Gil C., Andrew P.C., Detection of conformational isomers of anglerfish peptide YG (aPY) by reversed phase chromatography, J. Peptide Res., 34, 1989, 158-160.
  • [3] Meek J.L., Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition, Proceedings of the National Academy of Sciences of the United States of America, 77, 1980, 1632-1636.
  • [4] Purcell A.W., Aguilar M.I., Hearn M.T., High-performance liquid chromatography of amino acids, peptides, and proteins. XC. Investigations into the relationship between structure and reversed-phase high-performance liquid chromatography retention behavior of peptides related to human growth hormone, Journal of Chromatography, 476, 1989, 113-123.
  • [5] Sane S.U., Cramer S.M., Przybycien T.M., Protein structure perturbations on chromatographic surfaces, Journal of Chromatography, A 849, 1999, 149-159.
  • [6] McNay J.L.M., Fernandez E.J., Protein unfolding during reversed-phase chromatography, II. Role of salt type and ionic strength, Biotechnology and Bioengineering 76, 2001, 233-240.
  • [7] McNay J.L.M., O'Connell J.P., Fernandez E.J., Protein unfolding during reversed-phase chromatography, I. Effect of surface properties and duration of adsorption, Biotechnology and Bioengineering 76, 2001, 224-232.
  • [8] Karger B.L., Blanco R., The effect of on-column structural changes of proteins on their HPLC behavior, Talanta 36, 1989, 243-248.
  • [9] Nucci M.L., Shorr R., Abuchowski A., Strategies for dealing with the immunogenicity of therapeutic proteins, Handbook of Experimental Pharmacology (Novel Therapeutics from Modern Biotechnology), 137, 1999, 59-88.
  • [10] Kendrick M.L., Kerwin B.A., Chang B.S., Philo J.S., Online size-exclusion high-performance liquid chromatography light scattering and differential refractometry methods to determine degree of polymer conjugation to proteins and protein-protein or protein-ligand association states, Analytical Biochemistry, 299, 2001, 136-146.
  • [11] Kinstler O.B., Brems D.N., Lauren S.L., Scott L., Paige A.G., Hamburger J.B., Treuheit M.J., Characterization and stability of N-terminally PEGylated rhG-CSF, Dep. Pharmaceutics Drug Delivery, Amgen Incorp. Thousand Oaks, CA, USA. Pharmaceutical Research, 13, 1996, 996-1002.
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-BGPK-1042-4109
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.