Спонтанный протеолитический процессинг рекомбинантного антимюллерова гормона человека: структурные и функциональные различия молекулярных форм.

А.Я. Рак, А.В. Трофимов, Е.А. Протасов, А.В. Жахов, Я.А. Забродская, А.М. Ищенко

Research output: Contribution to journalArticle


The technology of obtaining of highly purified human recombinant anti-mullerian hormone (AMH) – a potential antitumor agent for the therapy of certain types of malignant neoplasms – is described. It was found that during the storage of AMH preparations under physiological conditions, spontaneous proteolytic processing of the hormone is possible. It leads to the formation of C-terminal homodimer of AMH (activated form), and then, during the further proteolysis, an inactive state. Sites, for 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 its C-terminal fragment, contained in the preparations, are analyzed.
Original languageRussian
Pages (from-to)25-33
Issue number1
StatePublished - 2019
Externally publishedYes


  • amh
  • anti-mullerian hormone
  • chromatography
  • MALDI mass-spectrometry
  • MALDI масс-спектрометрия
  • monoclonal antibodies
  • proteolysis
  • recombinant protein
  • АМГ
  • антимюллеров гормон
  • моноклональные антитела
  • протеолиз
  • рекомбинантный белок
  • хроматография

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