MOLECULAR-KINETIC PROPERTIES OF CRYSTALLINE TRYPSINOGEN

Crystalline Chymo-trypsin and Chymo-trypsinogen

A new crystalline protein, chymo-trypsinogen, has been isolated from acid extracts of fresh cattle pancreas. This protein is not an enzyme but is transformed by minute amounts of trypsin into an active proteolytic enzyme called chymo-trypsin. The chymo-trypsin has also been obtained in crystalline form. The chymo-trypsinogen cannot be activated by enterokinase, pepsin, inactive trypsin, or calc...

Formation of Trypsin from Crystalline Trypsinogen by Means of Enterokinase

Crystalline trypsinogen is most readily and completely transformed into trypsin by means of enterokinase in the range of pH 5.2-6.0 at 5 degrees C. and at a concentration of trypsinogen of not more than 0.1 mg. per ml. The action of enterokinase under these conditions is that of a typical enzyme. The process follows closely the course of a catalytic unimolecular reaction, the rate of formation ...

Molecular kinetic and electrophoretic properties of bacteriophages.

Molecular and kinetic properties of Aspergillus ficuum inulinases.

The beta-fructosidases from the thermotolerant fungus, A. ficuum, were characterized. All were active as to inulin and sucrose hydrolysis with different specificity constants (kcat/Km). The enzymes were classified according to the ratio (alpha) of the specificity constants for inulin (I) and sucrose (S). The invertase showed an alpha value of lower than one, while the inulinases had alpha value...

Kinetic properties and molecular size of thrombin-activated favtor V.

Native bovine factor V exists in three forms of differing molecular size, the oligomeric interconvertible forms A and C and a phospholipid-containing complex designated form L. Thrombin increases the activity of form A to a greater extent than form L and does not alter the activity of form C. Thrombin-activated form A and form C function as potent inhibitors of thrombin activation of form A but...