Crystalline Human Urokinase: Some Properties
- 19 February 1965
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 147 (3660), 880-882
- https://doi.org/10.1126/science.147.3660.880
Abstract
Human urokinase, an enzyme which activates plasminogen, has been crystallized. Repeated recrystallization yielded preparations of maximum specific activity; such preparations revealed only one component when subjected to polyacrylamide gel disc electrophoresis. Studies with the ultracentrifuge demonstrated that urokinase undergoes a concentration-dependent reversible association at pH 6.8. When the partial specific volume of the enzyme is assumed to be 0.735 milliliters per gram at 10°C, Archibald measurements indicate the molecular weight of urokinase to be 53,000.Keywords
This publication has 12 references indexed in Scilit:
- Present status of thrombolytic therapyAmerican Heart Journal, 1964
- The Present Status of Fibrinolytic TherapyAngiology, 1963
- Fibrinolytic mechanisms and the development of thrombolytic therapyAmerican Journal Of Medicine, 1962
- Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide GelsNature, 1962
- The biochemistry and physiology of urokinaseThe American Journal of Cardiology, 1960
- The preparation of human urokinaseThe American Journal of Cardiology, 1960
- Urokinase an activator of plasminogen from human urine I. Isolation and propertiesBiochimica et Biophysica Acta, 1957
- [2] Ultracentrifugation, diffusion, and viscometryPublished by Elsevier ,1957
- Simultaneous Determination of Molecular Weights and Sedimentation ConstantsThe Journal of Physical Chemistry, 1955
- An Activator of Plasminogen in Normal Urine.Experimental Biology and Medicine, 1952