Russian Journal of Bioorganic Chemistry, volume 36, issue 6, pages 696-703
Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain
Sharapova O A
1
,
Pozdnyakova N V
1
,
Laurinavichyute D K
2
,
Yurkova M S
2
,
Posypanova G A
3
,
Andronova S M
2
,
Fedorov A. N.
2
,
Severin S. E.
1
,
Severin E S.
2
1
Moscow Research Institute of Medicinal Ecology, Moscow, Russia
|
2
All-Russian Research Center of Molecular Diagnosis and Therapy, Moscow, Russia
|
Publication type: Journal Article
Publication date: 2010-11-18
Quartile SCImago
Q4
Quartile WOS
Q4
Impact factor: 1
ISSN: 10681620, 1608330X
Organic Chemistry
Biochemistry
Abstract
Alpha-fetoprotein (AFP) is the major human oncofetal protein. The receptor of AFP is expressed by cells of various tumors and is not produced by normal cells of the adult body. In an AFP molecule, the site of binding to its receptor is localized in the third domain. The conjugates of the natural AFP with a variety of cytostatics inhibited the growth of tumor cells in vivo and in vitro. The C-terminal fragment of AFP (amino acid residues 404–595 of the full-length protein) was cloned and expressed in cells of the Escherichia coli strain BL21(DE3). The yield of the protein was no less than 150 mg/l. A highly efficient method of its isolation and renaturation was developed so that the yield of the protein was no less than 50% with a purity of about 93%. The renatured third domain of AFP bound specifically to and penetrated into cells having the AFP receptor. The recombinant third domain of AFP can be used as a carrier for targeted drug delivery to tumor cells.
Citations by journals
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1
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Annales Pharmaceutiques Francaises
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Annales Pharmaceutiques Francaises
1 publication, 50%
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Russian Chemical Reviews
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Russian Chemical Reviews
1 publication, 50%
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1
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Citations by publishers
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1
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Elsevier
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Elsevier
1 publication, 50%
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Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii
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Autonomous Non-profit Organization Editorial Board of the journal Uspekhi Khimii
1 publication, 50%
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1
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Sharapova O. A. et al. Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain // Russian Journal of Bioorganic Chemistry. 2010. Vol. 36. No. 6. pp. 696-703.
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Sharapova O. A., Pozdnyakova N. V., Laurinavichyute D. K., Yurkova M. S., Posypanova G. A., Andronova S. M., Fedorov A. N., Severin S. E., Severin E. S. Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain // Russian Journal of Bioorganic Chemistry. 2010. Vol. 36. No. 6. pp. 696-703.
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TY - JOUR
DO - 10.1134/S106816201006004X
UR - https://doi.org/10.1134%2FS106816201006004X
TI - Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain
T2 - Russian Journal of Bioorganic Chemistry
AU - Sharapova, O A
AU - Pozdnyakova, N V
AU - Laurinavichyute, D K
AU - Yurkova, M S
AU - Posypanova, G A
AU - Andronova, S M
AU - Fedorov, A. N.
AU - Severin, S. E.
AU - Severin, E S.
PY - 2010
DA - 2010/11/18 00:00:00
PB - Pleiades Publishing
SP - 696-703
IS - 6
VL - 36
SN - 1068-1620
SN - 1608-330X
ER -
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@article{2010_Sharapova,
author = {O A Sharapova and N V Pozdnyakova and D K Laurinavichyute and M S Yurkova and G A Posypanova and S M Andronova and A. N. Fedorov and S. E. Severin and E S. Severin},
title = {Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain},
journal = {Russian Journal of Bioorganic Chemistry},
year = {2010},
volume = {36},
publisher = {Pleiades Publishing},
month = {nov},
url = {https://doi.org/10.1134%2FS106816201006004X},
number = {6},
pages = {696--703},
doi = {10.1134/S106816201006004X}
}
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MLA
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Sharapova, O. A., et al. “Isolation and characterization of the recombinant human α-fetoprotein fragment corresponding to the C-terminal structural domain.” Russian Journal of Bioorganic Chemistry, vol. 36, no. 6, Nov. 2010, pp. 696-703. https://doi.org/10.1134%2FS106816201006004X.