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Primary Structure of Human Fibrinogen and Fibrin

I. CLEAVAGE OF FIBRINOGEN WITH CYANOGEN BROMIDE. ISOLATION AND CHARACTERIZATION OF NH2-TERMINAL FRAGMENTS OF THE agr("A") CHAIN

Birger Blombäck 1, Birgit Hessel 1, Sadaaki Iwanaga 1, Jan Reuterby 1, and Margareta Blombäck 1

From the 1 From the Department of Blood Coagulation Research, Karolinska Institutet, 104 01 Stockholm, Sweden

The cleavage of human fibrinogen in 70% formic acid with CNBr has been studied. A fragment containing the NH2-terminal portions of the three chains has been obtained from the reaction mixture. After reduction and alkylation the NH2-terminal fragments of the agr(A) and agr(AP) chains have been isolated in essentially pure form by gel filtration and chromatography. The amino acid sequence of these fragments has been determined. Evidence is presented for the occurrence in the agr(A) and agr(AP) chain preparations of the chain variants agr(AY) and agr(AYP).

The relation between structure and function of fibrinogen is discussed.

Submitted on February 1, 1971


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