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. 1975 Mar;145(3):469–474. doi: 10.1042/bj1450469

Purification and some characteristics of the coagulation factor IX from human plasma.

B Osterud, R Flengsrud
PMCID: PMC1165246  PMID: 1171684

Abstract

Non-activated coagulation factor IX was purified approx. 10,000-fold from human plasma. The final product was electrophoretically homogeneous and comprised a tingle polypeptide chain with a molecular weight of about 70,000 and a pI of 4.3-4.45. The N-terminal amino acid was glycine. The amino acid and the carbohydrate contents were analysed and a monospecific antiserum to the factor was raised in rabbits.

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