Autor: |
Yakar, S., Kaplan, B., Livneh, A., Martin, B., Miura, K., Ali-Khan, Z., Shtrasburg, S., Pras, M. |
Předmět: |
|
Zdroj: |
Scandinavian Journal of Immunology; Dec1994, Vol. 40 Issue 6, p653-658, 6p, 1 Chart |
Abstrakt: |
To study the mechanism of amyloid deposition, the nature of amyloid proteins formed in experimental murine amyloidosis, was examined. Spleen specimens, 15-60 mg, were homogenized and extracted using aqueous acidic acetonitrile, in a recently developed procedure, making it possible to obtain amyloid proteins from minute amounts of tissue. The extracted material, 1.5-4mg, was analysed by Western blotting and ELISA using antibodies recognizing differentially proteins AA and SAA. Two immunoreactive proteins of 8 and 12 KDa were isolated and subjected to amino acid analysis and N-terminal sequence determination. The results of immunochemical and chemical examination showed that the 8 and 12 KDa proteins represented proteins AA and SAA, respectively. The data obtained provide new direct evidence for SAA deposition in tissues during murine amyloidogenesis. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
|