Amino Acid Structures of Multiple Forms of Amyloid-Related Serum Protein SAA from a Single Individual

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Multiple forms of the acute-phase serum protein SAA were isolated from the lipoprotein fraction of plasma from a single individual. These protein forms were purified by size-exclusion, ion-exchange, and reverse-phase high-pressure liquid chromatography, and then the tryptic peptides were subjected to amino acid sequence analysis. A total of three distinct 104-residue proteins were identified. Two of these proteins differed only by having either an arginine or a histidine at position 71 while the third protein had seven amino acid differences. Each of these proteins has a 103-residue companion protein where the amino-terminal arginine has been removed. Two of these protein sequences match the two human SAA cDNA structures reported in the literature. The presence of three unique amino acid sequences in one individual is proof that there must be a minimum of two genes for SAA in humans.

Original languageEnglish (US)
Pages (from-to)1677-1682
Number of pages6
JournalBiochemistry
Volume27
Issue number5
DOIs
StatePublished - Mar 1 1988

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Serum Amyloid A Protein
Amino Acids
Proteins
Arginine
High pressure liquid chromatography
Acute-Phase Proteins
Ion Exchange
Protein Sequence Analysis
Reverse-Phase Chromatography
Histidine
Lipoproteins
Blood Proteins
Amino Acid Sequence
Ion exchange
Complementary DNA
Genes
High Pressure Liquid Chromatography
Plasmas
Peptides

ASJC Scopus subject areas

  • Biochemistry

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Amino Acid Structures of Multiple Forms of Amyloid-Related Serum Protein SAA from a Single Individual. / Dwulet, Francis E.; Wallace, David K.; Benson, Merrill D.

In: Biochemistry, Vol. 27, No. 5, 01.03.1988, p. 1677-1682.

Research output: Contribution to journalArticle

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