Results 121 to 130 of about 193,488 (165)
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Serum Amyloid A Isoforms in Inflammation

Scandinavian Journal of Immunology, 1991
Serum amyloid A protein (SAA) was extracted from serum using hydrophobic interaction chromatography and four or six isoforms were separated by isoelectric‐focusing. These represented three pairs of isoforms, each with and without an N‐terminal arginine. SAA I (pi 6.1). SAA l des‐arg (pl 5.9).
J G, Raynes, K P, McAdam
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Serum amyloid a in carcinoma of the lung

Cancer, 1986
Serum concentrations of serum amyloid A protein (SAA), peripheral blood lymphocytes (PBL) mitogenic response to phytohemagglutinin (PHA) and Concanavalin A (Con A), numbers of circulating T- and B-lymphocytes and length of survival after diagnosis were measured in 50 patients with cancer of the lung. SAA levels were significantly elevated when compared
M D, Benson, S, Eyanson, N S, Fineberg
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Immune Functions of Serum Amyloid A

Critical Reviews in Immunology, 2012
Serum amyloid A (SAA) is a highly conserved, acute-phase protein synthesized predominantly by the liver. After secretion into the circulation, it associates with high-density lipoprotein (HDL) particles. During acute inflammation, serum SAA levels may rise up to 1000-fold, and under these conditions, SAA displaces apolipoprotein A-I from HDL, thus ...
Kari K, Eklund, K, Niemi, P T, Kovanen
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Serum amyloid A in autoimmune thrombosis

Autoimmunity Reviews, 2006
The objectives of this study were (1) to determine how levels of serum amyloid A (SAA), high sensitivity C-reactive protein (CRP) and interleukin-6 (IL-6) correlate to autoimmune diseases in patients with or without thrombosis, and (2) to discuss the parameters that influence the relative SAA values.
S, Sodin-Semrl   +6 more
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Degradation of serum amyloid A and apolipoproteins by serum proteases

Biochemistry, 1984
We have investigated the protease activity, present in human serum, that digests the serum amyloid A (SAA) protein. SAA radiolabeled with 125I was incubated at 37 degrees C with serum and plasma and analyzed for degradation products by alkaline urea-polyacrylamide gel electrophoresis and gel filtration chromatography.
L L, Bausserman, P N, Herbert
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Degradation of Serum Amyloid A in Amyloid‐Susceptible and Amyloid‐Resistant Mouse Strains

Scandinavian Journal of Immunology, 1996
Degradation of serum amyloid A (apoSAA) by resident peritoneal cells (RPCS) and conditioned medium (CDM), prepared with RPCS, from amyloid‐susceptible CBA/J mice, amyloid‐resistant CE/J mice and their amyloid‐resistant CBA/J × CE/J F1 progeny was investigated in vitro.
R, Elliott-Bryant   +3 more
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Serum Amyloid A (SAA) Proteins

2020
As normal constituents of blood serum, the Serum Amyloid A (SAA) proteins are small (104 amino acids in humans) and remarkably well-conserved in mammalian evolution. They are synthesized prominently, but not exclusively, in the liver. Fragments of SAA can associate into insoluble fibrils (called "amyloid") characteristic of "secondary" amyloid disease ...
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The Primary Structure of Serum Amyloid A Protein in the Sheep: Comparison with Serum Amyloid A in Other Species

Scandinavian Journal of Immunology, 1994
Serum amyloid A (SAA) protein was isolated from acute phase sheep sera by ultracentrifugation, gel filtration and ion‐exchange chromatography. The purified protein was characterized by sodium dodecylsulfate polyacrylamidc gel electrophoresis (SDS‐PAGE), isoelectric focusing, amino acid composition and Edman degradation.
P V, Syversen   +4 more
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SERUM AMYLOID A

Journal of Hypertension, 2004
E. Hatanaka   +3 more
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Binding of serum-derived amyloid-associated proteins to amyloid fibrils

Amyloid: the International Journal of Experimental and Clinical Investigation: the Official Journal of the International Society of Amyloidosis, 2023
Konen Obayashi   +2 more
exaly  

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