Surface properties of fibrinogen and fibrin
CJ Van Oss - Journal of protein chemistry, 1990 - Springer
CJ Van Oss
Journal of protein chemistry, 1990•SpringerBy contact angle measurements on layers of fibrinogen and fibrin, it can be shown that the
transformation from fibrinogen to fibrin is accompanied by a change in surface properties
from very hydrophilic (fibrinogen) to moderately but definitely hydrophobic (fibrin). It is also
shown that, contrary to serum albumin and gamma globulin, fibrinogen does not become
more hydrophobic upon drying.
transformation from fibrinogen to fibrin is accompanied by a change in surface properties
from very hydrophilic (fibrinogen) to moderately but definitely hydrophobic (fibrin). It is also
shown that, contrary to serum albumin and gamma globulin, fibrinogen does not become
more hydrophobic upon drying.
Abstract
By contact angle measurements on layers of fibrinogen and fibrin, it can be shown that the transformation from fibrinogen to fibrin is accompanied by a change in surface properties from very hydrophilic (fibrinogen) to moderately but definitely hydrophobic (fibrin). It is also shown that, contrary to serum albumin and gamma globulin, fibrinogen does not become more hydrophobic upon drying.
Springer