( 624 ) 
Of the indentity of the fibringlobulin which is obtained by the 
coagulation by ferment and that which is found in filtrate after the 
heat-coagulation of the fibrinogen, there is no doubt, on account of 
the conformity in composition, coagulation temperature ete. When 
however it must be assumed that the fibringlobulin is already before- 
hand present in the fibrinogensolutions, then for the present falls 
away every ground to assume that by the clotting by ferment the 
fibringlobulin should be formed still in another way e.g. by trans- 
formation of fibrinogen, the more so, as the quantity of fibringlo- 
bulin which is obtained by clotting with ferment certainly is com- 
paratively not larger than that which can be prepared by heating 
from a fibrinogensolution. HAMMARSTEN ') found, it is true, that in 
weak alkaline solutions relatively little fibrin was formed by ferment 
and so relatively much proteid remained dissolved; this may partly 
be explained by the fact that the fibringlobulin was disintregrated 
very completely by the alkaline reaction, partly also, as HAMMARSTEN 
himself observes, by the fact, that under these circumstances part of 
the fibrin remained dissolved as “soluble fibrin”. 
From the fact that a solution of fibrinogen, from which the fibrin- 
globulin is removed by means of Nall, clots with fibrinferment, must 
be deduced that by removal of the fibringlobulin the fibrinogen 
proper is not, as might be expected from the formula given by 
SCHMIEDEBERG and defended a short time ago by HeuBNer *) changed 
into fibrin, and that in general the fibringlobulin does not play a 
considerable part in the clotting. So the clottingprocess must consist 
in an alteration of the fibrinogenmolecule itself. That fibringlobulin 
is present in the serum of coagulated fibrinogensolutions can be 
easily explained from this, that fibringlobulin was found already in 
free condition in greater or smaller quantities in the fibrinogensolu- 
tion, so the supposition, that the ferment causes a splitting off of 
fibringlobulin is superfluous as may be deduced from this. 
Physics. — “The transformation of a branch plait into a main 
plait and vice versa.” By Prof. J. D. van per Waars. 
If for a binary mixture the temperature is raised above the critical 
temperature of one of the components, the y-surface has a plait, 
which does not occupy the whole breadth from «=0O to «=1, 
but which is closed on the side of the component for which 7%, 
lies below the chosen value of 7. In normal cases such a plait 
1) Pfliigers Archiv, Bd. 30, p. 479. 
2) Arch. f. exp. Pathol. u. Pharmakol. Bd. 49, p. 229. 
