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• W2131211557 startingPage "657" @default.
• W2131211557 abstract "Serum amyloid A protein (SAA) was extracted from serum using hydrophobic interaction chromatography and four or six isoforms were separated by isoelectric-focusing. These represented three pairs of isoforms, each with and without an N-terminal arginine. SAA I (pi 6.1). SAA l des-arg (pl 5.9). SAA2α (pi 6.9) and SAAα: des-arg (pl 6.6) were found to be present in all individuals from Europe and the USA. A minority of these individuals (11 of 56) expressed SAA2/β (pl 7. 1) and SAA2/β des-arg (pi 6.8). Serum from patients in Papua New Guinea and Malawi both showed a much higher frequency ofSAA2/β. There was no indication of altered isoforms in regions with high incidence of reactive AA amyloidosis. In sequential serum samples, concentrations of des-arg isoforms were found to reach a maximum 0 24 h later than isoforms with an arginine. Concentrations of the isoform SAA1 decreased faster in five of six patients (16±:7.5 h to decrease 50%) than SAAl des-arg (22± 11 h to decrease 50%). Variations in the handling of N-terminal arginine may be important for the formation-susceptibility of amyloid deposits." @default.
• W2131211557 created "2016-06-24" @default.
• W2131211557 creator A5018637989 @default.
• W2131211557 creator A5086324955 @default.
• W2131211557 date "1991-06-01" @default.
• W2131211557 modified "2023-09-25" @default.
• W2131211557 title "Serum Amyloid A Isoforms in Inflammation" @default.
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• W2131211557 doi "https://doi.org/10.1111/j.1365-3083.1991.tb02538.x" @default.
• W2131211557 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2047759" @default.
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