Analysis of Some Biochemical Properties of Recombinant Siberian Roe Deer (Capreolus pygargus) Chymosin Obtained in the Mammalian Cell Culture (CHO-K1)-Reference-Cited by-同舟云学术

Analysis of Some Biochemical Properties of Recombinant Siberian Roe Deer (Capreolus pygargus) Chymosin Obtained in the Mammalian Cell Culture (CHO-K1)

Published:2023-09 Issue:9 Volume:88 Page:1284-1295
ISSN:0006-2979
Container-title:Biochemistry (Moscow)
language:en
Short-container-title:Biochemistry Moscow

Author:

Murashkin Denis E.,Belenkaya Svetlana V.,Bondar Aleksandr A.,Elchaninov Vadim V.,Shcherbakov Dmitrii N.

Publisher

Pleiades Publishing Ltd

Subject

Biochemistry,General Medicine,Biochemistry, Genetics and Molecular Biology (miscellaneous),Biophysics,Geriatrics and Gerontology

Link

https://link.springer.com/content/pdf/10.1134/S0006297923090080.pdf

Reference43 articles.

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2. Khan, A. R., Khazanovich-Bernstein, N., Bergmann, E. M., and James, M. N. (1999) Structural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursors, Proc. Natl. Acad. Sci. USA, 96, 10968-10975, https://doi.org/10.1073/pnas.96.20.10968.

3. Richter, C., Tanaka, T., and Yada, R. Y. (1998) Mechanism of activation of the gastric aspartic proteinases: pepsinogen, progastricsin and prochymosin, Biochem. J., 335, 481-490, https://doi.org/10.1042/bj3350481.

4. Chen, H., Zhang, G., Zhang, Y., Dong, Y., and Yang, K. (2000) Functional implications of disulfide bond, Cys206-Cys210, in recombinant prochymosin (chymosin), Biochemistry, 39, 12140-12148, https://doi.org/10.1021/bi000976o.

5. Eskandari, M. H., Hosseini, A., Alasvand Zarasvand, S., and Aminlari, M. (2012) Cloning, expression, purification and refolding of caprine prochymosin, Food Biotechnol., 26, 143-153, https://doi.org/10.1080/08905436.2012.670829.

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