Lactate Dehydrogenase Monoclonal Antibody Sandwich ELISA To Determine Cooking Temperature of Ground Beef

1996 ◽  
Vol 44 (12) ◽  
pp. 4048-4051 ◽  
Author(s):  
A. Orta-Ramirez ◽  
C. H. Wang ◽  
M. M. Abouzied ◽  
G. J. Veeramuthu ◽  
J. F. Price ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Lactate Dehydrogenase ◽  
Sandwich Elisa ◽  
Ground Beef ◽  
Cooking Temperature

Lactate Dehydrogenase Polyclonal Antibody Sandwich ELISA for Determination of Endpoint Heating Temperatures of Ground Beef

1996 ◽  
Vol 59 (1) ◽  
pp. 51-55 ◽  
Author(s):  
CHENG-HSIN WANG ◽  
MOHAMED M. ABOUZIED ◽  
JAMES J. PESTKA ◽  
DENISE M. SMITH
Keyword(s):  
Lactate Dehydrogenase ◽  
Polyclonal Antibody ◽  
Heating Temperature ◽  
Polyclonal Antibodies ◽  
Sandwich Elisa ◽  
Ground Beef ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Marker ◽  
Beef Patties

An enzyme-linked immunosorbent assay (ELISA) for the protein marker lactate dehydrogenase (LDH) was developed to determine endpoint heating temperature (EPT) of ground beef. Ground beef was placed in 10 by 75 mm tubes and heated to temperatures between 62 and 74°C at 2°C intervals. Electrophoresis and immunoblotting of meat extracts indicated a decrease in the intensity of the LDH band as temperature was increased. Polyclonal antibodies (PAb) against bovine muscle LDH were produced and a sandwich ELISA devised using biotinylated PAb as the detecting antibody. The LDH content decreased (P < 0.05) in ground beef heated between 66 and 74°C and was less than 4 μg/g of meat at the recommended minimum endpoint of 69°C. The ELISA was used to estimate the EPT of commercially cooked beef patties.

scholarly journals Detection of Mycoplasma agalactiae Antigen in Sheep and Goats by Monoclonal Antibody-Based Sandwich ELISA

2004 ◽  
Vol 73 (4) ◽  
pp. 461-464 ◽  
Author(s):  
D. Zendulková ◽  
H. J. Ball ◽  
A. Madanat ◽  
P. Lány ◽  
Z. Pospíšil
Keyword(s):  
Monoclonal Antibody ◽  
Sandwich Elisa ◽  
Mycoplasma Agalactiae ◽  
Sheep And Goats

Development of a monoclonal antibody against the left wing of ciguatoxin CTX1B: Thiol strategy and detection using a sandwich ELISA

Toxicon ◽  
2012 ◽  
Vol 60 (3) ◽  
pp. 348-357 ◽  
Author(s):  
Takeshi Tsumuraya ◽  
Katsutoshi Takeuchi ◽  
Shuji Yamashita ◽  
Ikuo Fujii ◽  
Masahiro Hirama
Keyword(s):  
Monoclonal Antibody ◽  
Sandwich Elisa ◽  
Left Wing

Residual Triose Phosphate Isomerase Activity and Color Measurements to Determine Adequate Cooking of Ground Beef Patties†

1999 ◽  
Vol 62 (2) ◽  
pp. 156-161 ◽  
Author(s):  
ARNIE I. SAIR ◽  
ALDEN M. BOOREN ◽  
BRADFORD W. BERRY ◽  
DENISE M. SMITH
Keyword(s):  
Frozen Storage ◽  
Ground Beef ◽  
Past Research ◽  
Triose Phosphate Isomerase ◽  
Department Of Agriculture ◽  
Freeze Thaw ◽  
Triose Phosphate ◽  
Isomerase Activity ◽  
Beef Patties ◽  
Cooking Temperature

The objectives were to (i) compare the use of triose phosphate isomerase (TPI) activity and internal color scores for determination of cooking adequacy of beef patties and (ii) determine the effect of frozen storage and fat content on residual TPI activity in ground beef. Ground beef patties (24.4% fat) were cooked to five temperatures ranging from 60.0 to 82.2°C. TPI activity decreased as beef patty cooking temperature was increased from 60.0 to 71.1°C; however, no difference (P > 0.05) in activity (6.3 U/kg meat) was observed in patties cooked to 71.1°C and above. Degree of doneness color scores, a* values and b* values, of ground beef patties decreased as internal temperature was increased from 60.0 to 71.1°C; however, temperature had no effect on L* values. TPI activity in raw ground beef after five freeze–thaw cycles did not differ from the control. Three freeze–thaw cycles of raw ground beef resulted in a 57.2% decrease in TPI activity after cooking. TPI activity of cooked beef increased during 2 months of frozen storage, but TPI activity in ground beef stored for 3 months or longer did not differ from the unfrozen control. While past research has shown color to be a poor indicator of adequate thermal processing, our results suggest that undercooked ground beef patties could be distinguished from those that had been adequately cooked following U.S. Department of Agriculture guidelines using residual TPI activity as a marker.

scholarly journals PRRSV Vaccine Strain-Induced Secretion of Extracellular ISG15 Stimulates Porcine Alveolar Macrophage Antiviral Response against PRRSV

Viruses ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 1009
Author(s):  
Hongbin Liu ◽  
Bingjun Shi ◽  
Zhigang Zhang ◽  
Bao Zhao ◽  
Guangming Zhao ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Vaccine Strain ◽  
Sandwich Elisa ◽  
Respiratory Syndrome Virus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Porcine Alveolar Macrophage ◽  
Type I ◽  
Swine Industry ◽  
Host Interactions ◽  
Isg15 Expression

Porcine reproductive and respiratory syndrome virus (PRRSV) has disrupted the global swine industry since the 1980s. PRRSV-host interactions are largely still unknown but may involve host ISG15 protein. In this study, we developed a monoclonal antibody (Mab-3D5E6) specific for swine ISG15 (sISG15) by immunizing mice with recombinant sISG15. A sandwich enzyme-linked immunosorbent assay (ELISA) incorporating this sISG15-specific Mab was developed to detect sISG15 and provided a lower limit of sISG15 detection of 200 pg/mL. ELISA results demonstrated that infection of porcine alveolar macrophages (PAMs) with low-virulence or attenuated PRRSV vaccine strains induced intracellular ISG15 expression that was independent of type I IFN production, while PAMs infection with a PRRSV vaccine strain promoted extracellular ISG15 secretion from infected PAMs. Conversely, the addition of recombinant sISG15 to PAMs mimicked natural extracellular ISG15 effects whereby sISG15 functioned as a cytokine by activating PAMs. Once activated, PAMs could inhibit PRRSV replication and resist infection with PRRSV vaccine strain TJM. In summary, a sandwich ELISA incorporating homemade anti-ISG15 Mab detected ISG15 secretion induced by PAMs infection with a PRRSV vaccine strain. Recombinant ISG15 added to cells exhibited cytokine-like activity that stimulated PAMs to assume an anti-viral state that enabled them to inhibit PRRSV replication and resist viral infection.

Monoclonal antibodies specific for prothrombin fragment 1.2 and their use in a quantitative enzyme-linked immunosorbent assay

1993 ◽  
Vol 39 (4) ◽  
pp. 583-591 ◽  
Author(s):  
M J Hursting ◽  
B T Butman ◽  
J P Steiner ◽  
B M Moore ◽  
M C Plank ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Human Plasma ◽  
Sandwich Elisa ◽  
Peptide Sequence ◽  
Carboxyl Terminus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Thrombotic Risk ◽  
Prothrombin Fragment ◽  
Amino Terminal

Abstract Prothrombin fragment 1.2 (F1.2) is an activation peptide generated during a critical event of blood coagulation, the conversion of prothrombin to thrombin. As a marker of thrombin generation, F1.2 has clinical potential in assessing thrombotic risk and monitoring anticoagulant therapy. In developing a highly specific, monoclonal antibody-based immunoassay of human plasma F1.2, we generated six murine anti-F1.2 monoclonal antibodies, using as immunogen a synthetic peptide (sequence: CGSD-RAIEGR) similar to the unique carboxyl terminus of F1.2. Each antibody bound F1.2 but not prothrombin. Epitope mapping studies with one antibody (5-3B) showed that optimum binding required six to eight amino acids plus a terminal arginine to emulate the F1.2 carboxyl terminus. A quantitative sandwich ELISA for human plasma F1.2 was configured with monoclonal antibody 5-3B as the capture antibody and peroxidase-labeled polyclonal antibodies to the F1.2 amino-terminal region as detector antibodies. Calibrators were prepared by adding purified F1.2, 0-10 nmol/L, to F1.2-depleted plasma. Assay characteristics included the following: mean (+/- SD) analytical recovery of 98% +/- 13%; no interference from lipemia, hemolysis, icterus, or thrombolytic agents; 0.08 nmol/L sensitivity; and mean intra- and interassay imprecision (three lots) < 12% at both low and high concentrations of F1.2.

A Sensitive Monoclonal Antibody Sandwich ELISA for the Measurement of the Major Olive Pollen Allergen Ole e 1

2000 ◽  
Vol 122 (3) ◽  
pp. 224-228 ◽  
Author(s):  
Ronald van Ree ◽  
Marja Aalbers ◽  
Olga Kea ◽  
Francisco M. Marco de la Calle ◽  
José M. Sempere Ortells ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Sandwich Elisa ◽  
Pollen Allergen ◽  
Olive Pollen

Production of monoclonal antibodies for Plasmodium vivax lactate dehydrogenase and patient sera screening using sandwich ELISA

2012 ◽  
Vol 111 (4) ◽  
pp. 1645-1650 ◽  
Author(s):  
Jong-Hyun Kim ◽  
Jinyoung Lee ◽  
Hae-Jin Sohn ◽  
Hyun-Ok Song ◽  
Jung-Yeon Kim ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Lactate Dehydrogenase ◽  
Plasmodium Vivax ◽  
Sandwich Elisa
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