Proteinase resistance of carnosine, pyrrolylcarnosine, and salicylcarnosine
- Авторлар: Shevchenko K.V.1, Nagaev I.Y.1, Kulikova O.I.2, Stvolinsky S.L.2, Shevchenko V.P.1, Myasoedov N.F.1
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Мекемелер:
- National Research Centre “Kurchatov Institute”
- Research Center of Neurology
- Шығарылым: Том 50, № 2 (2024)
- Беттер: 146-152
- Бөлім: Articles
- URL: https://innoscience.ru/0132-3423/article/view/670957
- DOI: https://doi.org/10.31857/S0132342324020042
- EDN: https://elibrary.ru/ONHXKY
- ID: 670957
Дәйексөз келтіру
Аннотация
The stability of carnosine, pyrrolylcarnosine (PC) and salicylcarnosine (SC) to the action of leucine aminopeptidase, carboxypeptidases B and Y was evaluated. It was found that proteolysis of carnosine, PC and SC under the action of leucine aminopeptidase does not occur. Carboxypeptidases B and Y, as well as the enzyme system of blood plasma and plasma membranes of rat brain cells, degraded peptides containing β-alanyl, N-pyrrolyl, N-salicylic fragments to varying degrees. In all cases, histidine is formed. The formation of pyrrole or salicylic acid does not occur. It was found that carnosine, PC and SC showed high stability to the action of amino- and carboxypeptidases in in vitro experiments.
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Толық мәтін

Авторлар туралы
K. Shevchenko
National Research Centre “Kurchatov Institute”
Хат алмасуға жауапты Автор.
Email: ATCarma@mail.ru
Ресей, 123182, Moscow, pl. Kurchatova 2
I. Nagaev
National Research Centre “Kurchatov Institute”
Email: ATCarma@mail.ru
Ресей, 123182, Moscow, pl. Kurchatova 2
O. Kulikova
Research Center of Neurology
Email: ATCarma@mail.ru
Ресей, 125367, Moscow, Volokolamskoe shosse 80
S. Stvolinsky
Research Center of Neurology
Email: ATCarma@mail.ru
Ресей, 125367, Moscow, Volokolamskoe shosse 80
V. Shevchenko
National Research Centre “Kurchatov Institute”
Email: ATCarma@mail.ru
Ресей, 123182, Moscow, pl. Kurchatova 2
N. Myasoedov
National Research Centre “Kurchatov Institute”
Email: ATCarma@mail.ru
Ресей, 123182, Moscow, pl. Kurchatova 2
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