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Separation Of Protein C From Cohn Fraction Iv-1 By Mini-Antibody.

Authors :
Back, Nathan
Cohen, Irun R.
Lajtha, Abel
Lambris, John D.
Paoletti, Rodolfo
Maguire, David J.
Bruley, Duane F.
Harrison, David K.
Rezania, Samin
Ahn, Doh G.
Kang, Kyung A.
Source :
Oxygen Transport to Tissue XXVIII; 2008, p125-131, 7p
Publication Year :
2008

Abstract

Human protein C (PC) is a natural anticoagulant, antithrombotic, anti-inflammatory, and anti-apoptotic in the bloodstream. PC deficiency can lead to abnormal blood clot formation inside blood vessels, possibly causing heart attack, stroke, skin necrosis, or even death. PC can be, therefore, a valuable therapeutic with little side effect, unlike the currently used anti-coagulants. To reduce the cost involved in immuno purification of PC from blood plasma, single chain variable fragments (mini-Mab) are being produced by recombinantE. coli using phagemid technique. As an economic means of purifying the PC specific mini-Mab, metal affinity chromatography (IMAC) purification process was also investigated. Then using the purified mini-Mab, the feasibility of PC purification from the Cohn Fraction IV-1 was examined. Cohn Fraction IV-1 is usually a discarded side-stream from the blood plasma fractionation of human serum albumin. It holds 90% of PC in plasma, but is very cheap. Preliminary study of PC purification from the Cohn Fraction IV-1 showed 16% purification yield using mini-Mab immobilized NHS-activated Sepharose. The economic analysis for PC purification using mini-Mab showed that the overall process was found to be tens of times cheaper than that using Mab. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISBNs :
9780387717630
Database :
Supplemental Index
Journal :
Oxygen Transport to Tissue XXVIII
Publication Type :
Book
Accession number :
33172171
Full Text :
https://doi.org/10.1007/978-0-387-71764-7_17