Movatterモバイル変換

[0]ホーム
URL:

Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
Thehttps:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

NIH NLM Logo
Log inShow account info
Access keysNCBI HomepageMyNCBI HomepageMain ContentMain Navigation
pubmed logo
Advanced Clipboard
User Guide

Full text links

Free PMC article
Full text links

Actions

Share

.2009 Apr;1(1):47-51.

Production and purification of streptokinase by protected affinity chromatography

Affiliations

Production and purification of streptokinase by protected affinity chromatography

Mohammad Babashamsi et al. Avicenna J Med Biotechnol.2009 Apr.

Abstract

Streptokinase is an extracellular protein, extracted from certain strains of beta hemolytic streptococcus. It is a non-protease plasminogen activator that activates plasminogen to plasmin, the enzyme that degrades fibrin cloth through its specific lysine binding site; it is used therefore as a drug in thrombolytic therapy. The rate of bacterial growth and streptokinase production was studied in condition of excess glucose addition to culture media and its pH maintenance. The streptokinase product of the bacterial culture was preliminary extracted by salt precipitation and then purified by affinity chromatography on plasminogen substituted sepharose-4B in a condition that the plasminogen active site was protected from streptokinase-induced activation. The purity of streptokinase was confirmed by SDS-PAGE and its biological activity determined in a specific streptokinase assay. The results showed that in the fed-batch culture, the rate of streptokinase production increased over two times as compared with the batch culture while at the same time, shortening the streptokinase purification to a single step increased the yield over 95% at the chromatography stage.

Keywords: Affinity chromatography; Culture; Plasminogen; Purification; Streptokinase.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Evaluation of plasminogen purification by SDS-PAGE (Left to right): 1. MW marker 2. Elution dialyzed 3. Washing with 0.1 M phosphate buffer 4. Human plasma
Figure 2
Figure 2
Variation of streptokinase [production rate] in culture media by pH regulation and glucose addition
Figure 3
Figure 3
Evaluation of streptokinase purification by SDS-PAGE (Left to right): 1- MW marker 2- Ammonium sulfate extract 3-Purified and dialyzed streptokinase 4-BSA
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

References

    1. Tillet WS, Garner RL. The fibrinolytic activity of hemolytic streptococci's. J Exp Med. 1933;58(4):485–502. - PMC - PubMed
    1. Schick LA, Castellino F. Direct evidence for the generation of an active site in the plasminogen moiety of the streptokinase-human plasminogen activator complex. J Biochem Biophys Res Com-mun. 1974;57(1):47–54. - PubMed
    1. Hoffman R, Benz EJ, Jr, Shattil SJ. Hematology: Basic principles and practice. New York: Churchill Livingstone; 1991. (Eds)
    1. Rodriguez P, Fuentes P, Barro M, Alvarez JG, Muñoz E, Collen D, et al. Structural domains of streptokinase involved in the interaction with plasminogen. Eur J Biochem. 1995;229(1):83–90. - PubMed
    1. Hermentin P, Cuesta-Linker T, Weisse J, Schmidt KH, Scheld M, Thimme M. Comparative analysis of the activity and content of different streptokinase preparations. Eur H J. 2005;26(9):933–940. - PubMed

LinkOut - more resources

Full text links
Free PMC article
Cite
Send To

NCBI Literature Resources

MeSHPMCBookshelfDisclaimer

The PubMed wordmark and PubMed logo are registered trademarks of the U.S. Department of Health and Human Services (HHS). Unauthorized use of these marks is strictly prohibited.

[8]ページ先頭
©2009-2025 Movatter.jp