Spontaneous Proteolytic Processing of Human Recombinant Anti-Mullerian Hormone: Structural and Functional Differences of the Molecular Forms. Rak, A., Trofimov, A., Protasov, E., Rodin, S., Zhahov, A., Zabrodskaya, Y., & Ischenko, A. Applied Biochemistry and Microbiology, 55(1):13-20, Pleiades Publishing, 2019. cited By 1![Spontaneous Proteolytic Processing of Human Recombinant Anti-Mullerian Hormone: Structural and Functional Differences of the Molecular Forms [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Abstract: The technology for the production of highly purified human recombinant anti-mullerian hormone (AMH)—a potential antitumor agent for the treatment of certain types of malignant neoplasms—is described. It was found that spontaneous proteolytic processing of the hormone is possible during the storage of AMH preparations under physiological conditions. This leads to the formation of C-terminal homodimer of AMH (activated form) and, later, to an inactive state during the further proteolysis. Sites at which spontaneous processing of the hormone molecule occurred during prolonged storage with the formation of active and inactive fragments were identified. The structural and functional differences in the molecular forms of the C-terminal fragment contained in the preparations are analyzed. © 2019, Pleiades Publishing, Inc.
@ARTICLE{Rak201913,
author={Rak, A.Y. and Trofimov, A.V. and Protasov, E.A. and Rodin, S.V. and Zhahov, A.V. and Zabrodskaya, Y.A. and Ischenko, A.M.},
title={Spontaneous Proteolytic Processing of Human Recombinant Anti-Mullerian Hormone: Structural and Functional Differences of the Molecular Forms},
journal={Applied Biochemistry and Microbiology},
year={2019},
volume={55},
number={1},
pages={13-20},
doi={10.1134/S0003683819010149},
note={cited By 1},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063724530&doi=10.1134%2fS0003683819010149&partnerID=40&md5=e5de197b812d7a0bc61fbd16ada849b1},
affiliation={State Research Institute of Highly Pure Biopreparations, Federal Medical-Biological Agency (FMBA), St. Petersburg, 197110, Russian Federation; St. Petersburg State University, St. Petersburg, 199034, Russian Federation; Research Institute of Influenza, Ministry of Health of Russia, St. Petersburg, 197376, Russian Federation},
abstract={Abstract: The technology for the production of highly purified human recombinant anti-mullerian hormone (AMH)—a potential antitumor agent for the treatment of certain types of malignant neoplasms—is described. It was found that spontaneous proteolytic processing of the hormone is possible during the storage of AMH preparations under physiological conditions. This leads to the formation of C-terminal homodimer of AMH (activated form) and, later, to an inactive state during the further proteolysis. Sites at which spontaneous processing of the hormone molecule occurred during prolonged storage with the formation of active and inactive fragments were identified. The structural and functional differences in the molecular forms of the C-terminal fragment contained in the preparations are analyzed. © 2019, Pleiades Publishing, Inc.},
author_keywords={AMH; anti-mullerian hormone; chromatography; MALDI mass-spectrometry; monoclonal antibodies; proteolysis; recombinant protein},
correspondence_address1={Rak, A.Y.; State Research Institute of Highly Pure Biopreparations, Federal Medical-Biological Agency (FMBA)Russian Federation; email: rak@hpb-spb.com},
publisher={Pleiades Publishing},
issn={00036838},
language={English},
abbrev_source_title={Appl. Biochem. Microbiol.},
document_type={Article},
source={Scopus},
}
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