Version 1
: Received: 18 July 2024 / Approved: 19 July 2024 / Online: 19 July 2024 (10:52:36 CEST)
How to cite:
Lotay, N.; Suarez, C. M.; Franier, B. D. L.; Jockusch, R. A.; Thompson, M. Synthesis and Characterization of Recombinant Gelsolin 1-3 for Use in the Detection of Lysophosphatidic Acid, a Possible Ovarian Cancer Biomarker. Preprints2024, 2024071589. https://doi.org/10.20944/preprints202407.1589.v1
Lotay, N.; Suarez, C. M.; Franier, B. D. L.; Jockusch, R. A.; Thompson, M. Synthesis and Characterization of Recombinant Gelsolin 1-3 for Use in the Detection of Lysophosphatidic Acid, a Possible Ovarian Cancer Biomarker. Preprints 2024, 2024071589. https://doi.org/10.20944/preprints202407.1589.v1
Lotay, N.; Suarez, C. M.; Franier, B. D. L.; Jockusch, R. A.; Thompson, M. Synthesis and Characterization of Recombinant Gelsolin 1-3 for Use in the Detection of Lysophosphatidic Acid, a Possible Ovarian Cancer Biomarker. Preprints2024, 2024071589. https://doi.org/10.20944/preprints202407.1589.v1
APA Style
Lotay, N., Suarez, C. M., Franier, B. D. L., Jockusch, R. A., & Thompson, M. (2024). Synthesis and Characterization of Recombinant Gelsolin 1-3 for Use in the Detection of Lysophosphatidic Acid, a Possible Ovarian Cancer Biomarker. Preprints. https://doi.org/10.20944/preprints202407.1589.v1
Chicago/Turabian Style
Lotay, N., Rebecca Ann Jockusch and Michael Thompson. 2024 "Synthesis and Characterization of Recombinant Gelsolin 1-3 for Use in the Detection of Lysophosphatidic Acid, a Possible Ovarian Cancer Biomarker" Preprints. https://doi.org/10.20944/preprints202407.1589.v1
Abstract
Gelsolin is an actin-binding protein that is competitively bound by lysophosphatidic acid (LPA), a possible biomarker for the early detection of ovarian cancer. Our group has previously shown the usage of gelsolin 1-3 (a fragment of gelsolin composed of the first three of its six subdomains) along with actin to detect the presence of lysophosphatidic acid. This histidine-tagged gelsolin 1-3 fragment is synthesized in our lab using bl21 Rosetta cells but required further characterization. This study aims to provide sufficient characterization of gelsolin 1-3 synthesized in our lab via both sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and mass spectrometry using a Fourier-transform ion cyclotron resonance mass spectrometer (FTICR-MS). Both techniques show the presence of protein at the expected mass of approximately 41 kDa. Additionally, the dissociation of a smaller fragment of the complex when introduced into the gas phase which was equivalent to the approximate mass of one subdomain of gelsolin 1-3 further supports this conclusion.
Keywords
gelsolin; SDS-PAGE; FTICR-MS; mass spectrometry; protein characterization
Subject
Biology and Life Sciences, Life Sciences
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
