| Literature DB >> 7307348 |
Abstract
Human amyloid-related protein SAA has been prepared and purified by gel filtration, ion-exchange and affinity chromatography techniques. It was shown that SAA, even after extensive purification, is an electrophoretically heterogeneous protein. In addition, prealbumin and fragments of albumin were detected in the SAA preparation. Most of the SAA molecules and the fragments of albumin were present in a free form, but some SAA was also found to be complexed with albumin fragments.Entities:
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Year: 1981 PMID: 7307348 PMCID: PMC1537261
Source DB: PubMed Journal: Clin Exp Immunol ISSN: 0009-9104 Impact factor: 4.330