Polymorphism of Tissue and Serum Amyloid A (AA and SAA) Proteins in the Mouse
Open Access
- 1 July 1978
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Immunology
- Vol. 121 (1) , 138-140
- https://doi.org/10.4049/jimmunol.121.1.138
Abstract
Amino acid sequence studies of the amino terminal 25 residues of amyloid A (AA) protein and the serum precursor (SAA) induced with casein or LPS indicate differences in the sequence at position 6 and significant heterogeneity at several other positions in SAA. These findings suggest that SAA is a polymorphic serum protein and raise the possibility that only certain forms of SAA are processed to the tissue amyloid fibril.This publication has 6 references indexed in Scilit:
- BIOCHEMICAL EVIDENCE FOR BIPHASIC DEVELOPMENT OF EXPERIMENTAL AMYLOIDOSIS1978
- Kinetics of serum amyloid protein A in casein-induced murine amyloidosis.Journal of Clinical Investigation, 1977
- Amyloid-Related Serum Protein SAA from Three Animal Species: Comparison with Human SAAThe Journal of Immunology, 1977
- Murine model for human secondary amyloidosis: genetic variability of the acute-phase serum protein SAA response to endotoxins and casein.The Journal of Experimental Medicine, 1976
- The complete amino acid sequence of an amyloid fibril protein AA1 of unusual size (64 residues)Biochemical and Biophysical Research Communications, 1976
- The characterization of soluble amyloid prepared in waterJournal of Clinical Investigation, 1968