THE PURIFICATION OF HAPTOGLOBIN
- 1 June 1961
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry and Physiology
- Vol. 39 (6), 1013-1019
- https://doi.org/10.1139/o61-101
Abstract
A method for preparing haptoglobin in highly purified form from human serum is described. The serum is acidified to pH 4.6 and deionized by gel filtration. Under these conditions haptoglobin is selectively adsorbed from serum by diethyl-aminoethyl-cellulose. The protein is eluted with a dilute solution of sodium chloride, and impurities are removed by fractionation with ammonium sulphate. A partial purification of serum cholinesterase can be obtained by a similar method.Keywords
This publication has 12 references indexed in Scilit:
- Gel Filtration: A Method for Desalting and Group SeparationNature, 1959
- Human haptoglobins: estimation and purificationBiochemical Journal, 1959
- THE RENAL EXCRETION OF HEMOGLOBIN: REGULATORY MECHANISMS AND THE DIFFERENTIAL EXCRETION OF FREE AND PROTEIN-BOUND HEMOGLOBIN*†Journal of Clinical Investigation, 1959
- An improved procedure for starch-gel electrophoresis: further variations in the serum proteins of normal individualsBiochemical Journal, 1959
- Purification and properties of different haptoglobinsClinica Chimica Acta; International Journal of Clinical Chemistry, 1959
- Notation for Serum-Protein Groups and the Genes controlling their InheritanceNature, 1956
- A COMPARISON OF OPTICAL AND MANOMETRIC METHODS FOR THE ASSAY OF HUMAN SERUM CHOLINESTERASECanadian Journal of Biochemistry and Physiology, 1955