Human fibrinogen heterogeneity: the COOH-terminal residues of defective A alpha chains of fibrinogen II.

@article{Nakashima1992HumanFH,
  title={Human fibrinogen heterogeneity: the COOH-terminal residues of defective A alpha chains of fibrinogen II.},
  author={Akira Nakashima and Shoji Sasaki and Kentaro Miyazaki and Toshiyuki Miyata and Sadaaki Iwanaga},
  journal={Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis},
  year={1992},
  volume={3 4},
  pages={361-70}
}
Fibrinogen fraction I (340 kDa) and fraction II (305 kDa) were isolated by glycine precipitation. The subunit chains of the two fractions were separated, after reduction, by reverse-phase high performance liquid chromatography. The amino acid compositions of the B beta and tau chains of fibrinogen II were identical with those of fibrinogen I. In contrast, the A alpha chains of fibrinogen II were composed of two populations, one comprising homogeneous, intact A alpha chains and the other… CONTINUE READING