Gorevic P D, Levo Y, Frangione B, Franklin E C
J Immunol. 1978 Jul;121(1):138-40.
Amino acid sequence studies of the amino terminal 25 residues of amyloid A (AA) protein and the serum precursor (SAA) induced with casein or LPS indicate differences in the sequence at position 6 and significant heterogeneity at several other positions in SAA. These findings suggest that SAA is a polymorphic serum protein and raise the possibility that only certain forms of SAA are processed to the tissue amyloid fibril.
对由酪蛋白或脂多糖诱导产生的淀粉样蛋白A(AA)和血清前体(SAA)氨基末端25个残基的氨基酸序列研究表明,SAA在第6位的序列存在差异,且在其他几个位置存在显著的异质性。这些发现表明SAA是一种多态性血清蛋白,并增加了只有某些形式的SAA被加工成组织淀粉样纤维的可能性。