Abstract
Isoelectric identification of apo-SAA isoforms in mouse and human plasma is important in analyzing function and involvement in amyloidogenesis. In this paper we show the influence of altering the pH gradient on the migration of the human isoforms and identify novel minor apo-SAA isoforms. The NH2-terminals of these isoforms are analyzed by sequencing of the isoforms electroblotted onto polyvinylidene difluoride (PVDF) membranes. Integrity of the COOH-terminal is confirmed by blotting using a rabbit anti-human apo-SAA (aa 95-104) antibody. Isoelectric focusing (IEF) is compared to urea-SDS-acrylamide gel electrophoresis for the analysis of apo-SAA isoforms in haplotype A and B mouse strains [1,2].
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