IMPROVING PURIFICATION OF COAGULATION F IX USING HEPARIN AFFINITY CHROMATOGRAPHY AND ITS COMPARISON 
WITH ION EXCHANGE CHROMATOGRAPHY

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MUSAVI MOTLAGH S.SH.; REZVAN H.; MOUSAVI HOSSEINI M.K.; POURFATH ELAH A.A.

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Paper Information

Journal: THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON) Year:2005 | Volume:2 | Issue:4 Page(s): 91-98

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Title

IMPROVING PURIFICATION OF COAGULATION F IX USING HEPARIN AFFINITY CHROMATOGRAPHY AND ITS COMPARISON WITH ION EXCHANGE CHROMATOGRAPHY

Author(s)

MUSAVI MOTLAGH S.SH. | REZVAN H. | MOUSAVI HOSSEINI M.K. | POURFATH ELAH A.A. | Issue Writer Certificate

Keywords

HEPARIN AFFINITY CHROMATOGRAPHYQ4

FACTOR IXQ3

HEMOPHILIA BQ3

ION EXCHANGE CHROMATOGRAPHYQ4

Abstract

Background and Objectives Hemophilia B is a genetic disorder due to deficiency or complete absence of FACTOR IX coagulation factor. Treatment of choice for these patients is use of FACTOR IX concentrates. Therefore, purification of plasma proteins and separation of FACTOR IX have been major objectives for scientists involved in this field. In this respect, purification procedure using ION EXCHANGE CHROMATOGRAPHY is widely used, but in the past decade affinity chromatography was also introduced. The objective of the present study has been to apply both techniques for the purification of FACTOR IX and compare the quality and yield of the product. Materials and Methods For the purification procedure, chromatography columns (XK-16), containing DEAE sepharose and Heparin sepharose were used. FACTOR IX coagulation activity was measured using a one-stage coagulation assay and FACTOR IX antigen was quantified using ELISA technique. Results The specific activity and relative increase in purity of FACTOR IX was calculated and it was demonstrated that specific activity improved from 3.1 IU/mg using DEAE ion exchange to 29 IU/mg when affinity chromatography was added and purity was increased from 155 to 1450 respectively. Conclusions The present study demonstrates that addition of an affinity chromatography step using heparin sepharose is a major improvement in the purification of FACTOR IX, where both specific activity and purity are increased considerably.

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APA: Copy

MUSAVI MOTLAGH, S.SH., REZVAN, H., MOUSAVI HOSSEINI, M.K., & POURFATH ELAH, A.A.. (2005). IMPROVING PURIFICATION OF COAGULATION F IX USING HEPARIN AFFINITY CHROMATOGRAPHY AND ITS COMPARISON WITH ION EXCHANGE CHROMATOGRAPHY . THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON), 2(4), 91-98. SID. https://sid.ir/paper/78723/en

Vancouver: Copy

MUSAVI MOTLAGH S.SH., REZVAN H., MOUSAVI HOSSEINI M.K., POURFATH ELAH A.A.. IMPROVING PURIFICATION OF COAGULATION F IX USING HEPARIN AFFINITY CHROMATOGRAPHY AND ITS COMPARISON WITH ION EXCHANGE CHROMATOGRAPHY . THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON)[Internet]. 2005;2(4):91-98. Available from: https://sid.ir/paper/78723/en

IEEE: Copy

S.SH. MUSAVI MOTLAGH, H. REZVAN, M.K. MOUSAVI HOSSEINI, and A.A. POURFATH ELAH, “IMPROVING PURIFICATION OF COAGULATION F IX USING HEPARIN AFFINITY CHROMATOGRAPHY AND ITS COMPARISON WITH ION EXCHANGE CHROMATOGRAPHY ,” THE SCIENTIFIC JOURNAL OF IRANIAN BLOOD TRANSFUSION ORGANIZATION (KHOON), vol. 2, no. 4, pp. 91–98, 2005, [Online]. Available: https://sid.ir/paper/78723/en

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