| Literature DB >> 8137804 |
C F Bruun1, K Sletten, G Husby, G Marhaug.
Abstract
Using hydrophobic interaction chromatography, two-dimensional electrophoresis with an immobilized pH gradient in the first dimension and semidry blotting, three isoforms of mink serum amyloid A protein (SAA) were characterized and studied during chronic inflammation. Compared to conventional methods that have been applied to SAA, the major advantages of the present combination of methods are: (i) use of small serum volumes, (ii) rapid extraction, (iii) high resolution, and (iv) high yield of proteins.Entities:
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Year: 1993 PMID: 8137804 DOI: 10.1002/elps.11501401211
Source DB: PubMed Journal: Electrophoresis ISSN: 0173-0835 Impact factor: 3.535