Purification of haptoglobin and α2-macroglobulin from human serum

✍ Scribed by Charles J. Betlach; Donald E. McMillan

• Publisher: Elsevier Science
• Year: 1972
• Tongue: English
• Weight: 332 KB
• Volume: 49
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(72)90246-1

✦ Synopsis

Human serum glycoproteins are synthesized by the immunological system or by hepatic parenchymal cells. Immune globulins are present in reasonable concentration, especially when plasma cell myeloma is present, making their isolation in quantity from individual subjects fairly simple. Glycoproteins of hepatic origin are usually present in lower concentration, and methods for their isolation usually result in lower yield or greater impurity. For this reason, they have usually been isolated from pooled human plasma, rather than from the serum of individual subjects. Studies of glycoproteins of hepatic origin have t'herefore described average values for plasma pools but not individual variation in parameters such as protein-bound carbohydrate content. In the single exception to this situation, al-acid glycoprotein has been isolated from individual human subjects (1) and its carbohydrate content and other properties studied. We have modified previously reported methods (2-6) to develop a technique for isolating two additional glycoproteins, haptoglobin and cu,-macroglobulin, in reasonable quantity and purity from 10 ml of serum, an amount conveniently obtained from individual study subjects.