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• W2040997104 abstract "Recombinant tick anticoagulant peptide (r-TAP), a potent and specific inhibitor of blood coagulation factor Xa, was purified to greater than 99% homogeneity at the multi-gram scale. Genetically engineered yeast secreted 200-250 mg/l of the heterologous protein into the medium. Cells were separated from broth by diafiltration and purification was done by two chromatographic steps, both conducive to operation on a large scale. Analysis of the purified protein by several methods indicated that it was greater than 99% homogeneous and no incompletely processed or truncated proteins were detected. Physico-chemical characterization data of r-TAP show that it exists as a monomer in solution and no evidence of post-translational modification was observed. The purified protein was fully active in inhibiting human coagulation factor Xa." @default.
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• W2040997104 date "1992-02-01" @default.
• W2040997104 modified "2023-09-26" @default.
• W2040997104 title "Large-scale purification and characterization of recombinant tick anticoagulant peptide" @default.
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• W2040997104 doi "https://doi.org/10.1016/0378-4347(92)80034-n" @default.
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