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PMID: 63517 Published · ppublish English Comparative Study Journal Article

Amyloid-related serum protein SAA from three animal species: comparison with human SAA.

Journal of immunology (Baltimore, Md. : 1950) ·Vol. 118 ·No. 1 ·1977-01-00 ·Pages 229-34

Anders RF, Natvig JB, Sletten K, Husby G, Nordstoga K

Abstract

The amyloid-relates serum protein SAA has been isolated by gel filtration in 10% formic acid from three animal species: mink, mouse, rabbit. Sera used in the isolation procedure were obtained from animals in which high concentrations of SAA had been induced by treatment with LPS. The isolated SAA proteins had a subunit size similar to that of human SAA, with m.w. values ranging from 10,000 to 11,700 (estimated by gel filtration in 6 M guanidine-HC1) or 12,400 to 15,000 (estimated by SDS-PAGE). The m.w. studies and amino acid sequence data indicated that SAA and the amyloid fibril protein AA in the mouse, and probably also the mink, are related in the same way as in man, the two proteins having common NH2-terminal amino acid sequences and SAA being extended by 20 to 40 residues at the COOH-terminal end of the molecule.

MeSH Terms
Alpha-Globulins/immunology Amino Acid Sequence Amino Acids/analysis Amyloid/blood,immunology Animals Blood Proteins/isolation & purification Cross Reactions Humans Mice/blood Mink/blood Molecular Weight Rabbits/blood Species Specificity
Chemicals
Alpha-Globulins Amino Acids Amyloid Blood Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Anders R F
Natvig J B
Sletten K
Husby G
Nordstoga K
Article Info
Journal
Journal of immunology (Baltimore, Md. : 1950)
Abbr.
J Immunol
ISSN
0022-1767
Published
1977-01-00
Pages
229-34
Language
English
Region
United States
NLM ID
2985117R
Subset
IM
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