The complete amino acid sequence of bovine serum amyloid protein a (SAA) and of subspecies of the tissue-deposited amyloid fibril protein a

Rossevatin, K.; Andresen, P.K.; Sletten, K.; Husebekk, A.; Husby, G.; Nordstoga, K.; Johnson, K.H.; Westermark, G.T.; Westermark, P.

Scandinavian Journal of Immunology 35(2): 217-224

1992


ISSN/ISBN: 0300-9475
PMID: 1738817
DOI: 10.1111/j.1365-3083.1992.tb02853.x
Accession: 041595476

Download citation:  
Text
  |  
BibTeX
  |  
RIS

Article/Abstract emailed within 0-6 h
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

Abstract
Bovine serum amyloid A (SAA) was isolated from the acute phase high density lipoprotein (HDL) fraction of a cow suffering from acute mastitis. The elucidated primary structure revealed a protein consisting of 112 amino acid residues. Compared with SAA proteins from other species, the bovine protein was shown to have an insertion of nine amino acid residues between positions 69 and 70. No microheterogeneity could be observed in the protein. Amyloid fibrils extracted from the kidneys were found to contain at least three subspecies of protein AA, consisting of 68, 81 and about 110 amino acid residues. The amino acid sequences established for the protein AA subspecies revealed no microheterogeneity, and were identical to that elucidated for protein SAA.

The complete amino acid sequence of bovine serum amyloid protein a (SAA) and of subspecies of the tissue-deposited amyloid fibril protein a