<abstract xml:lang="en" xmlns="http://www.w3.org/1999/xhtml"><p>The stability of proteins is a subject of intense current interest. Aggregation, as a dominant degradation pathway for therapeutic proteins, may cause multiple adverse effects, including loss of efficacy and immunogenicity. In the present study, the formation of aggregates in lenograstim under physiological conditions was monitored. For this purpose, a simple and selective size-exclusion high-performance liquid chromatography method for detection and separation of aggregates from intact protein was developed. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis was performed under reducing and non-reducing conditions to determine the nature of aggregate bond formation. Using both techniques, the presence of a low aggregate content attached <italic>via</italic> disulfide bonds was detected.</p></abstract>

The stability of proteins is a subject of intense current interest. Aggregation, as a dominant degradation pathway for therapeutic proteins, may cause multiple adverse effects, including loss of efficacy and immunogenicity. In the present study, the formation of aggregates in lenograstim under physiological conditions was monitored. For this purpose, a simple and selective size-exclusion high-performance liquid chromatography method for detection and separation of aggregates from intact protein was developed. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis was performed under reducing and non-reducing conditions to determine the nature of aggregate bond formation. Using both techniques, the presence of a low aggregate content attached via disulfide bonds was detected.

Studying the formation of aggregates in recombinant human granulocyte-colony stimulating factor (rHuG-CSF), lenograstim, using size-exclusion chromatography and SDS-PAGE

Faculty of Pharmacy, University >Ss Cyril and Methodius<, 1000 Skopje, Macedonia

Acta Pharmaceutica

The stability of proteins is a subject of intense current interest. Aggregation, as a dominant degradation pathway for therapeutic proteins, may cause multiple...

Studying the formation of aggregates in recombinant human granulocyte-colony stimulating factor (rHuG-CSF), lenograstim, using size-exclusion chromatography and SDS-PAGE

Pubblicato online: 30 mag 2008

Pagine: 199 - 206

DOI: https://doi.org/10.2478/v10007-008-0003-6

Parole chiave
lenograstim, stvaranje agregata, tekućinska kromatografija visoke djelotvornosti isključenjem prema veličini, natrij-dodecil sulfat poliakrilamidna gel elektroforeza

This content is open access.

Studying the formation of aggregates in recombinant human granulocyte-colony stimulating factor (rHuG-CSF), lenograstim, using size-exclusion chromatography and SDS-PAGE

Pubblicato online: 30 mag 2008

Pagine: 199 - 206

DOI: https://doi.org/10.2478/v10007-008-0003-6

Parole chiavelenograstim, stvaranje agregata, tekućinska kromatografija visoke djelotvornosti isključenjem prema veličini, natrij-dodecil sulfat poliakrilamidna gel elektroforeza

This content is open access.

Parole chiave
lenograstim, stvaranje agregata, tekućinska kromatografija visoke djelotvornosti isključenjem prema veličini, natrij-dodecil sulfat poliakrilamidna gel elektroforeza