Affiliations: Department of Biochemistry, Institute of Haematology and Blood Transfusion, Warsaw, Poland
Note: [] Corresponding author: Malgorzata Musielak, PhD, Dept. of Biochemistry, Institute of Haematology and Blood Transfusion, Chocimska 5 St., 00-957 Warsaw, Poland. Tel.: +48 22 848 95 15; Fax: +48 22 848 06 37; E-mail: musielak@ihit.waw.pl.
Abstract: Human fibrinogen (TF) has been separated into two fractions: F1 – homodimers with respect to the γ chain, and F2 – heterodimers composed of γA and γ′ polypeptides. Their rouleaux-inducing properties were as follows: (1) both, at the same concentration of 0.8%, were less effective than TF; (2) F1 produced larger rouleaux even under static conditions of a hemocytometer where F2 was silent; (3) F2 induced the process when a suspension was gently sheared between microscopic slides. Since the synthetic peptide γ′(414–427) inhibited the rouleau formation in a mixture with F2, the C-terminal amino acids of the γ′ polypeptide probably bind the molecule to the cell. The inhibition was feebly visible in the native ratio of F1/F2, implicating a compensatory effect of F1.
