Isolation, subunit structure, and proteolytic modification of bovine factor VIII.

Autor: Legaz ME, Weinstein MJ, Heldebrant CM, Davie EW
Jazyk: angličtina
Zdroj: Annals of the New York Academy of Sciences [Ann N Y Acad Sci] 1975 Jan 20; Vol. 240, pp. 43-61.
DOI: 10.1111/j.1749-6632.1975.tb53321.x
Abstrakt: A new method has been described for the isolation of factor VIII. The method results in a high yield of factor VIII that is homogeneous by several different criteria. The purified protein is very stable and is not dissociated in the presence of 1 M NaCl or 0.25 M CaCl2. The highly purified protein is readily activated and inactivated by various proteolytic enzymes, such as thrombin, plasmin, and trypsin. The molecular events that lead to the activation reaction, however, have not been established.
Databáze: MEDLINE