Abstract
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.
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© 1991 Springer Science+Business Media Dordrecht
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Rygg, M., Husby, G., Dowton, B., Marhaug, G. (1991). Primary Structure of Two Rabbit Serum Amyloid a Proteins (SAA) Based on cDNA Sequence. In: Natvig, J.B., et al. Amyloid and Amyloidosis 1990. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3284-8_10
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DOI: https://doi.org/10.1007/978-94-011-3284-8_10
Publisher Name: Springer, Dordrecht
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