Structure and Variation in the Human Serum Amyloid A Gene Family

1988 ◽  
pp. 259-263
Author(s):  
George H. Sack ◽  
C. Conover Talbot
Keyword(s):  
Gene Family ◽  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

Organization of the Region Encompassing the Human Serum Amyloid A (SAA) Gene Family on Chromosome 11p15.1

Genomics ◽  
1994 ◽  
Vol 23 (2) ◽  
pp. 492-495 ◽  
Author(s):  
Grant C. Sellar ◽  
Kathy Oghene ◽  
Shelagh Boyle ◽  
Wendy A. Bickmore ◽  
Alexander S. Whitehead
Keyword(s):  
Gene Family ◽  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

Molecular Analysis of the Human Serum Amyloid A (SAA) Gene Family

1989 ◽  
Vol 29 (1) ◽  
pp. 113-119 ◽  
Author(s):  
G. H. SACK ◽  
C. C. TALBOT ◽  
H. SEUANEZ ◽  
S. J. O'BRIEN
Keyword(s):  
Gene Family ◽  
Human Serum ◽  
Molecular Analysis ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Structure of the murine serum amyloid A gene family. Gene conversion.

1986 ◽  
Vol 261 (18) ◽  
pp. 8442-8452 ◽  
Author(s):  
C A Lowell ◽  
D A Potter ◽  
R S Stearman ◽  
J F Morrow
Keyword(s):  
Gene Family ◽  
Gene Conversion ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Family Gene

Genetic Isofocusing Variant of Human Serum Amyloid A

1991 ◽  
pp. 20-23
Author(s):  
A. Steinmetz ◽  
H. Vitt ◽  
S. Motzny ◽  
H. Kaffarnik
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

scholarly journals Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

1989 ◽  
Vol 263 (2) ◽  
pp. 365-370 ◽  
Author(s):  
A F Strachan ◽  
E G Shephard ◽  
D U Bellstedt ◽  
G A Coetzee ◽  
D R van der Westhuyzen ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Gel Filtration ◽  
Density Lipoprotein ◽  
High Titre ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Buffer Solutions ◽  
Wide Range ◽  
Serum Amyloid A Protein

Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (greater than 90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at greater than 7 M-urea. By immunizing with apo-SAA adsorbed to acid-treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

Structural requirements of glycosaminoglycans for facilitating amyloid fibril formation of human serum amyloid A

Amyloid ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Aki Yamamoto ◽  
Shiori Watanabe ◽  
Sanae Takahashi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Structural Requirements ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Effect of amino acid variations in the central region of human serum amyloid A on the amyloidogenic properties

2014 ◽  
Vol 444 (1) ◽  
pp. 92-97 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Sachiko Miyagawa ◽  
Toshiyuki Yamada ◽  
Takahiro Mukai
Keyword(s):  
Amino Acid ◽  
Human Serum ◽  
Central Region ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A
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