Blood, 1960, Vol. 15, No. 1, pp. 164-173.
© 1960 American Society of Hematology, Inc.
Dysproteinemia Induced in Vitro by Plasmin
Digestion of Fibrinogen
E. KOWALSKI 1,
A. BUDZY
SKI 1,
M. KOPEC 1, and
K. MURAWSKI 1
1 Institute of Hematology and the Institute of Nuclear Research, Warsaw, Poland.
1. Electrophoretic investigation of split products of plasmin digestion
of pure fibrinogen and of fibrinogen in a plasma medium was performed.
It was shown that split products possessed electrophoretic mobilities of
alpha, beta and gamma globulins.
2. It could be shown that by digestion of I131-labeled fibrinogen, radioactivity in the range of alpha, beta and gamma globulins is released.
3. Simultaneously with the formation of high molecular intermediates,
low molecular, TCA-soluble substances are released.
4. Radioactivity balance calculation of the relative amounts of the newly
formed fractions has been performed.
5. A possible influence of plasmin-induced fibrinogen proteolysis on the
electrophoretic pattern of plasma proteins in dysproteinemia has been suggested.
6. The electrophoretic pattern of plasma proteins, obtained in the above
experiments is similar to those seen in patients with dysproteinemia.
Submitted on February 16, 1959
Accepted on April 10, 1959
