Primary structure of two rabbit serum amyloid a proteins (SAA) based on cDNA sequence

M. Rygg, G. Husby, B. Dowton, G. Marhaug

Research output: Chapter in Book/Report/Conference proceedingConference proceeding contributionpeer-review


The aim of this study was to predict the complete amino acid sequence of rabbit serum amyloid protein A (SAA) and identify heterogenities and amyloidogenic isotypes. After stimulation with turpentine a SAA specific mRNA signal was detected in the rabbit liver, and a cDNA library was made. Selected clones were sequenced. The deduced amino acid sequences of two rabbit SAA proteins differ in five amino acid residues, four of which are located in the NH2-terminal part. Only one of these two isotypes, SAA2, seems to be involved in amyloid formation.
Original languageEnglish
Title of host publicationAmyloid and amyloidosis 1990
Subtitle of host publicationVIth international symposium on amyloidosis August 5–8, 1990, Oslo, Norway
EditorsJacob B. Natvig, Øystein Førre, Gunnar Husby, Anne Husebekk, Bjørn Skogen, Knut Sletten, Per Westermark
Place of PublicationDordrecht
PublisherSpringer, Springer Nature
Number of pages4
ISBN (Electronic)9789401132848
ISBN (Print)9789401054508
Publication statusPublished - 1991
Externally publishedYes
EventVIth International Symposium on Amyloidosis - Oslo, Norway
Duration: 5 Aug 19908 Aug 1990


ConferenceVIth International Symposium on Amyloidosis


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