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The complete amino acid sequences of two related AA proteins (Mr 9700 and 5300) derived from thyroid tissue from a patient, NOR, with the autosomal recessive disease familial Mediterranean fever were determined. Heterogeneity found at position 52 indicates these proteins are fragments of two allelic or isotypic SAA precursor molecules similarly degraded at unusual sites and deposited in the thyroid. Degradation appears to be tissue and/or enzyme(s) specific since the carboxy terminus of both fragments is Ala-Ala and is different from other AA amyloid fibrils extracted from various tissues in different patients. Electron micrographic studies reveal these fragments retain the characteristics of native amyloid fibrils under physiological conditions even after exposure to dissociating agents.
Authors : Prelli F , Pras M , Frangione B ,
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WP101: Synthesis and Degradation of Ketone Bodies
WP1015: Synthesis and Degradation of Ketone Bodies
WP1079: Proteasome Degradation
WP1134: Synthesis and Degradation of Ketone Bodies
WP1196: Proteasome Degradation
WP1240: Proteasome Degradation
WP1451: Valine, leucine and isoleucine degradation
WP158: Proteasome Degradation
WP1612: 1,2-Dichloroethane degradation
WP1613: 1,4-Dichlorobenzene degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1615: 3-Chloroacrylic acid degradation
WP1623: Atrazine degradation
WP1626: Benzoate degradation via CoA ligation
WP1627: Benzoate degradation via hydroxylation
WP1632: Biphenyl degradation
WP1633: Bisphenol A degradation
WP1636: Caprolactam degradation
WP1637: Carbazole degradation
WP1646: Ethylbenzene degradation
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WP1654: gamma-Hexachlorocyclohexane degradation
WP1655: Geraniol degradation
WP1665: Limonene and pinene degradation
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