Amperometric Titration of -SH Groups in Purified Clotting Factors By Improved Method
- 1 March 1956
- journal article
- research article
- Published by Frontiers Media SA in Experimental Biology and Medicine
- Vol. 91 (3), 406-407
- https://doi.org/10.3181/00379727-91-22276
Abstract
The ethanol-ammoniacal amperometric method for quantitative measurement of -SH groups in proteins is susceptible to valid criticism. Previous work, employing this method, resulted in the inability to detect -SH groups in purified bovine prothrombin or its derivatives. Titration of these proteins by the new method described by Benesch, Lardy and Benesch, employing tris- (hydroxy-methylaminomethane) in aqueous, buffered solutions at pH 7.4, also resulted in the inability to detect -SH groups in these proteins.Keywords
This publication has 3 references indexed in Scilit:
- Concept of a Common Protein Moiety, Containing Disulfide Bonds, in Prothrombin, Prothrombin Derivative (Autoprothrombin) and ThrombinAmerican Journal of Physiology-Legacy Content, 1955
- THE SULFHYDRYL GROUPS OF CRYSTALLINE PROTEINS .1. SOME ALBUMINS, ENZYMES, AND HEMOGLOBINS1955
- Evaluation of Disulfide Bonds and Sulfhydryl Groups in the Blood Clotting MechanismAmerican Journal of Physiology-Legacy Content, 1954