Quantification of serum amyloid P by enzyme-linked immunosorbent assay

1991 ◽  
Vol 37 (10) ◽  
pp. 1742-1745 ◽  
Author(s):  
R Saïle ◽  
A Kandoussi ◽  
M Deveaux ◽  
J Descamps ◽  
E Hachulla ◽  
...  
Keyword(s):  
Human Plasma ◽  
Immunosorbent Assay ◽  
Polyclonal Antibodies ◽  
Serum Amyloid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Serum Amyloid P ◽  
Assay Procedure ◽  
Normal Individuals ◽  
Sandwich Type ◽  
Amyloid P

Abstract This enzyme-linked immunosorbent assay procedure for quantifying serum amyloid P (SAP) in human plasma makes use of affinity-purified polyclonal antibodies to SAP in a "sandwich"-type format. The procedure is sensitive, reproducible, simple, and easily automatable. Results correlate well with those by a rocket immunoelectrophoresis method performed with the same antibodies. Sera from apparently normal individuals had a mean SAP content of 44.17 mg/L and increased with age.

Proteomic characterization of novel serum amyloid P component variants from human plasma and urine

PROTEOMICS ◽  
2004 ◽  
Vol 4 (6) ◽  
pp. 1825-1829 ◽  
Author(s):  
Urban A. Kiernan ◽  
Dobrin Nedelkov ◽  
Kemmons A. Tubbs ◽  
Eric E. Niederkofler ◽  
Randball W. Nelson
Keyword(s):  
Human Plasma ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Human Plasma And Urine ◽  
Amyloid P

A Sandwich Enzyme-Linked Immunosorbent Assay for the Detection of Almonds in Foods†

2000 ◽  
Vol 63 (2) ◽  
pp. 252-257 ◽  
Author(s):  
JASON J. HLYWKA ◽  
SUSAN L. HEFLE ◽  
STEVE L. TAYLOR
Keyword(s):  
Immunosorbent Assay ◽  
Polyclonal Antibodies ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecylsulfate ◽  
Food Samples ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Sesame Seeds ◽  
Quality Control Tool ◽  
Sandwich Type

An enzyme-linked immunosorbent assay was developed to detect almonds as potential allergenic contaminants in food. Polyclonal antibodies directed against roasted almonds were partially purified from immunized sheep and rabbits and used as capture and secondary antibodies, respectively, in a sandwich-type, 96-well plate format. Food samples and almond-spiked samples were extracted 1:10 in phosphate-buffered saline at 60°C for 2 h, centrifuged, and applied to wells coated with sheep anti-almond antibody. After incubation, washing, and the addition of rabbit anti-almond antibody, the amount of almond present was detected with the subsequent addition of goat anti-rabbit immunoglobulin G–alkaline phosphatase conjugate and p-nitrophenyl phosphate substrate. Plate absorbances were read at 410 nm, and standard curves were developed in all matrices to quantify unknowns. Antibodies developed were specific for almond; however, some cross-reactivity was observed with extracts of some tree nuts and sesame seeds. Sodium dodecylsulfate–polyacrylamide gel electrophoresis and Western immunoblotting indicated that sheep anti-almond antibody recognized proteins extracted from black walnuts, Brazil nuts, cashews, hazelnuts, macadamia nuts, pistachios, and sesame seeds in addition to those from almond. The assay was optimized to detect less than 1 ppm of almond and was used successfully to determine almond residues in cereal and chocolate without cross-reacting interferences. A retail survey of 20 brands of cereal demonstrated that the assay produced statistically consistent results. This assay provides a useful quality control tool for the food industry for the protection of consumers allergic to almonds.

Serum Amyloid P Component (SAP) Interactome in Human Plasma Containing Physiological Calcium Levels

Biochemistry ◽  
2017 ◽  
Vol 56 (6) ◽  
pp. 896-902 ◽  
Author(s):  
Ebbe Toftgaard Poulsen ◽  
Kata Wolff Pedersen ◽  
Anna Maria Marzeda ◽  
Jan J. Enghild
Keyword(s):  
Human Plasma ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

Elevation of bovine serum C-reactive protein and serum amyloid P component levels by lactation

1991 ◽  
Vol 58 (3) ◽  
pp. 257-261 ◽  
Author(s):  
Masami Morimatsu ◽  
Atsushi Watanabe ◽  
Kumiko Yoshimatsu ◽  
Toru Fujinaga ◽  
Masahiko Okubo ◽  
...  
Keyword(s):  
Bovine Serum ◽  
Serum Amyloid ◽  
Enzyme Linked Immunosorbent Assay ◽  
C Reactive Protein ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Lactating Cows ◽  
Serum Amyloid P Component ◽  
Amyloid P

SummaryC-reactive protein (CRP) and serum amyloid P component (SAP), which are known to increase in sera from humans and many other animals with acute inflammation caused by infection, toxic drug administration or injury, were previously purified from bovine serum. These serum levels were determined by enzyme-linked immunosorbent assay (ELISA) using specific antiserum to bovine CRP or SAP which was prepared by immunizing rabbits and goats with each purified protein. Among 68 healthy Holstein cows, 45 non-lactating cows had levels of CRP and SAP of 20·6±1·4 and 27·6 ± 1·3 μg/ml respectively; 23 lactating cows had higher levels of CRP and SAP (76·0±13·6 and 38·3±5·5 μg/ml respectively). In the latter group, there was a high correlation between milk yield and serum CRP levels (P <0·001). From these observations, it was assumed that lactation might stimulate CRP synthesis rather than SAP synthesis in bovine liver as an acute phase reaction, and that CRP might be called a lactation-associated protein.

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