PREPARATION AND PROPERTIES OF THE COFACTOR OF AN ACTH-INACTIVATING ENZYME SYSTEM FROM HUMAN BLOOD1
- 1 October 1961
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 69 (4), 728-734
- https://doi.org/10.1210/endo-69-4-728
Abstract
The isolation from human blood of a cofactor of an in vitro enzyme system inactivating ACTH is described. The cofactor accelerated the loss of activity of ACTH as measured by the Sayers and Sayers bioassay in the presence of either a blood protein fraction (Cohn III-O) or plasminogen. The ACTH-inactivating activity of the latter in the present system does not appear to be identical with its fibrinolytic action.Keywords
This publication has 5 references indexed in Scilit:
- THE DESTRUCTION OF GLUCAGON, ADRENOCORTICOTROPIN AND SOMATOTROPIN BY HUMAN BLOOD PLASMA*JCI Insight, 1959
- THE DETERMINATION OF SUGAR IN BLOOD AND SPINAL FLUID WITH ANTHRONE REAGENTJournal of Biological Chemistry, 1955
- The amino-acid sequence in the glycyl chain of insulin. 1. The identification of lower peptides from partial hydrolysatesBiochemical Journal, 1953
- INACTIVATION OF ADRENOCORTICOTROPIC HORMONE IN VITRO BY TISSUES*Endocrinology, 1952
- Preparation and Properties of Serum and Plasma Proteins. IV. A System for the Separation into Fractions of the Protein and Lipoprotein Components of Biological Tissues and Fluids1a,b,c,dJournal of the American Chemical Society, 1946