BIOLOGICAL ACTIVITY ANALYSIS OF NATIVE AND RECOMBINANT STREPTOKINASE USING CLOT LYSIS AND CHROMOGENIC SUBSTRATE ASSAY

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

MAHBOUBI ARASH; SADJADY SEYYED KAZEM; MIRZAEI SALEH ABADI MOHAMMAD; AZADI SAEED; SOLAIMANIAN ROYA

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Iranian Journal of Pharmaceutical Research Year:2012 | Volume:11 | Issue:4 Page(s): 1087-1093

Download Full-Text

View:

292

Download:

160

Cites:

Information Journal Paper

Title

BIOLOGICAL ACTIVITY ANALYSIS OF NATIVE AND RECOMBINANT STREPTOKINASE USING CLOT LYSIS AND CHROMOGENIC SUBSTRATE ASSAY

Author(s)

Keywords

NATIVE STREPTOKINASE

RECOMBINANT STREPTOKINASE

CLOT LYSIS

CHROMOGENIC SUBSTRATE

BIOLOGICAL ACTIVITY

Abstract

Determination of streptokinase activity is usually accomplished through two assay methods: a) CLOT LYSIS, b) CHROMOGENIC SUBSTRATE assay. In this study the BIOLOGICAL ACTIVITY of two streptokinase products, namely StreptaseÒ, which is a native product and HeberkinasaÒ, which is a recombinant product, was determined against the third international reference standard using the two forementioned assay methods. The results indicated that whilst the activity of StreptaseÒ was found to be 101±4% and 97±5% of the label claim with CLOT LYSIS and CHROMOGENIC SUBSTRATE assay respectively, for HeberkinasaÒ the potency values obtained were 42±5% and 92.5±2% of the label claim respectively. To shed some light on the reason for this finding, the n-terminal sequence of the streptokinase molecules present in the two products was determined. The results showed slight differences in the amino acid sequence of the recombinant product in comparison to the native one at the amino terminus. This finding supports those of other workers who found that n- terminal sequence of the streptokinase molecule can have significant effect on the activity of this protein.

Cites

No record.

References

No record.

Cite

APA: Copy

MAHBOUBI, ARASH, SADJADY, SEYYED KAZEM, MIRZAEI SALEH ABADI, MOHAMMAD, AZADI, SAEED, & SOLAIMANIAN, ROYA. (2012). BIOLOGICAL ACTIVITY ANALYSIS OF NATIVE AND RECOMBINANT STREPTOKINASE USING CLOT LYSIS AND CHROMOGENIC SUBSTRATE ASSAY. IRANIAN JOURNAL OF PHARMACEUTICAL RESEARCH (IJPR), 11(4), 1087-1093. SID. https://sid.ir/paper/288032/en

Vancouver: Copy

MAHBOUBI ARASH, SADJADY SEYYED KAZEM, MIRZAEI SALEH ABADI MOHAMMAD, AZADI SAEED, SOLAIMANIAN ROYA. BIOLOGICAL ACTIVITY ANALYSIS OF NATIVE AND RECOMBINANT STREPTOKINASE USING CLOT LYSIS AND CHROMOGENIC SUBSTRATE ASSAY. IRANIAN JOURNAL OF PHARMACEUTICAL RESEARCH (IJPR)[Internet]. 2012;11(4):1087-1093. Available from: https://sid.ir/paper/288032/en

IEEE: Copy

ARASH MAHBOUBI, SEYYED KAZEM SADJADY, MOHAMMAD MIRZAEI SALEH ABADI, SAEED AZADI, and ROYA SOLAIMANIAN, “BIOLOGICAL ACTIVITY ANALYSIS OF NATIVE AND RECOMBINANT STREPTOKINASE USING CLOT LYSIS AND CHROMOGENIC SUBSTRATE ASSAY,” IRANIAN JOURNAL OF PHARMACEUTICAL RESEARCH (IJPR), vol. 11, no. 4, pp. 1087–1093, 2012, [Online]. Available: https://sid.ir/paper/288032/en

Related Journal Papers

No record.

Related Seminar Papers

No record.

Related Plans

No record.

Recommended Workshops