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KMID : 0380219930260020172
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 2 p.172 ~ p.175
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Purification fo Streptokinase by Affinity Chromatography using Human Plasminogen
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Jeong Il Kim
Young Eun Lee/Jeong Su Jang and Si Myung Byun
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Abstract
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A preparation of streptokinase with high specific activity and high yield has been obtained in a convenient manner through affinity chromatography using intact human plasminogen in the presence of -amino-N-caproic acid( -ACA).
Human plasminogen was purified from Cohn fraction III by the affinity chromatography with L-lysine-substituted Sepharose CL-4B. This plasmiogen was used as a ligand for streptokinase affinity chromatography. PBS(pH7.4) and glycine (pH2.5) were used as washing and elution buffer, respectively. To obtain a single peak, -ACA was added to both washing and elution buffers. The function of -ACA is the prevention of streptokinase fragmentation during the plasminogen activation.
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