A sensitive microassay for the determination of hemolytic complement activity in bovine milk

1983 ◽  
Vol 5 (2) ◽  
pp. 177-184 ◽  
Author(s):  
B. Poutrel ◽  
J.P. Caffin
Keyword(s):  
Bovine Milk ◽  
Complement Activity ◽  
Hemolytic Complement Activity

scholarly journals Study of hemolytic activity and subfactors of complement in smokers intoxication

2019 ◽  
Author(s):  
Rojan Ghanim Al Allaf
Keyword(s):  
Hemolytic Activity ◽  
Normal Values ◽  
Control Group ◽  
Healthy Individuals ◽  
Complement Components ◽  
Complement Activity ◽  
Normal People ◽  
Hemolytic Complement Activity ◽  
Heavy Smokers

Abstract Heavy Smokers appeared to be less resistant to infection, such as bacteria, viruses, and parasites. Many studies have examined the complement components concentrations than compared with normal people and ignored the functional sequencing of complement components, our study included the determination of complement activity by using Sheep red blood cells (SRBCs) as antigen and extracting the hemolytic activity (50%) of complement compounds, and because of difficulty of this method we using statistical analysis program (SPSS 23) and derived the inverse equation which gives the decomposition percentage (1-100%) of complement components by using five serum dilutions only. The total hemolytic complement activity (CH50) and its C3 and C4 fractions were determined in 30 heavy smokers. The results were compared with a control group that contained 30 persons matched in age and sex. Generally, both C3 and C4 concentrations were increased in smoker's individual in compared with the control group. However, when the independent t-test has applied the differences in the C3 and C4 levels in the control group (healthy individuals) and in the smoker group were found to be statistically insignificant but the inverse equation showed a 7% reduction in CH50 in smokers compared with the control group, where 18% reduction was observed. Our current study suggests that the complement components of the heavy smokers suffer from a significant dysfunction in the function, although the concentration of the basic components in the serum is parallel with normal values.

Automated homogeneous liposome-based assay system for total complement activity

1995 ◽  
Vol 41 (4) ◽  
pp. 586-590 ◽  
Author(s):  
S Yamamoto ◽  
K Kubotsu ◽  
M Kida ◽  
K Kondo ◽  
S Matsuura ◽  
...  
Keyword(s):  
Serum Proteins ◽  
M Protein ◽  
Homogeneous Population ◽  
Complement Activity ◽  
Activity Test ◽  
Human Sera ◽  
Total Complement ◽  
Hemolytic Complement Activity ◽  
Glucose 6 Phosphate Dehydrogenase

Abstract We developed an automated homogeneous immunoassay, based on immune lysis of dinitrophenyl (DNP)-labeled liposomes, for measuring total complement activity. Liposome lysis caused by complement activity was detected spectrophotometrically from entrapped glucose-6-phosphate dehydrogenase activity. Complement activity in human sera was quantified by comparison with a calibration curve. For ease of application to fully automated routine clinical analyzers, we adopted a two-reagent system, one reagent containing a homogeneous population of small DNP-labeled liposomes and one containing antibody/substrate. This system required calibration only once a week. Within-run and between-run CVs were 0.4-1.3% (n = 10) and 1.8-4.7% (n = 10), respectively. Serum results were linear upon dilution (with saline) over a twofold range. Bilirubin, hemoglobin, Intrafat, and serum proteins such as rheumatoid factor, M protein, IgG, and IgA did not affect the assay results. The results (y) correlated well with those from a hemolytic complement activity test (x): y = 1.05x - 1.14, r = 0.92, on 66 samples in the range < 10- > 50 kU/L. This method should therefore be of great use for the determination of complement activity.

scholarly journals Study of hemolytic activity and subfactors of complement in smokers intoxication

2019 ◽  
Author(s):  
Rojan Ghanim Al Allaf
Keyword(s):  
Hemolytic Activity ◽  
Normal Values ◽  
Control Group ◽  
Healthy Individuals ◽  
Complement Components ◽  
Complement Activity ◽  
Normal People ◽  
Hemolytic Complement Activity ◽  
Heavy Smokers

Abstract Background: Heavy Smokers appeared to be less resistant to infection, such as bacteria, viruses, and parasites. Many studies have examined the complement components concentrations than compared with normal people and ignored the functional sequencing of complement components. Methods: our study included the determination of complement activity by using Sheep red blood cells (SRBCs) as antigen and extracting the hemolytic activity (50%) of complement compounds, and because of difficulty of this method we using statistical analysis program (SPSS 23) and derived the inverse equation which gives the decomposition percentage (1-100%) of complement components by using five serum dilutions only, The total hemolytic complement activity (CH50) and its C3 and C4 fractions were determined in 30 heavy smokers. Results: The results were compared with a control group that contained 30 persons matched in age and sex. Generally, both C3 and C4 concentrations were increased in smoker's individual in compared with the control group. However, when the independent t-test has applied the differences in the C3 and C4 levels in the control group (healthy individuals) and in the smoker group were found to be statistically insignificant but the inverse equation showed a 7% reduction in CH50 in smokers compared with the control group, where 18% reduction was observed. Conclusions: Our current study suggests that the complement components of the heavy smokers suffer from a significant dysfunction in the function, although the concentration of the basic components in the serum is parallel with normal values.

Rapid, sensitive and specific determination of oxytetracycline residues in bovine milk and meat by CAD MIKES analysis at the 1 ppb level

1985 ◽  
Vol 12 (9) ◽  
pp. 493-496 ◽  
Author(s):  
P. Traldi ◽  
S. Daolio ◽  
B. Pelli ◽  
R. Maffei Facino ◽  
M. Carini
Keyword(s):  
Bovine Milk ◽  
Specific Determination

Fluorometric determination of uric acid in bovine milk

2010 ◽  
Vol 77 (4) ◽  
pp. 438-444 ◽  
Author(s):  
Torben Larsen ◽  
Kasey M Moyes
Keyword(s):  
Heat Treatment ◽  
Uric Acid ◽  
Xanthine Oxidase ◽  
Bovine Milk ◽  
Oxidase Inhibitor ◽  
Enzymatic Oxidation ◽  
Fast Method ◽  
Xanthine Oxidase Inhibitor ◽  
Milk Samples

The primary objective of this study is to validate a new fast method for determination of uric acid in milk. The method is based on an enzymatic-fluorometric technique that requires minimal pre-treatment of milk samples. The present determination of uric acid is based on the enzymatic oxidation of uric acid to 5-hydroxyisourate via uricase where the liberated hydrogen peroxide reacts with 10-acetyl-3,7-dihydroxyphenoxazine via peroxidase and the fluorescent product, resorufin, is measured fluorometrically. Fresh composite milk samples (n=1,072) were collected from both Jersey (n=38) and Danish Holstein (n=106) cows from one local herd. The average inter- and intra-assay variations were 7·1% and 3·0%, respectively. Percent recovery averaged 103·4, 107·0 and 107·5% for samples spiked with 20, 40 or 60 μmof standard, respectively, with a correlation (r=0·98;P<0·001) observed between the observed and expected uric acid concentrations. A positive correlation (r=0·96;P<0·001) was observed between uric acid concentrations using the present method and a reference assay. Storage at 4°C for 24 h resulted in lower (P<0·01) uric acid concentrations in milk when compared with no storage or samples stored at −18°C for 24 h. Addition of either allopurinol (a xanthine oxidase inhibitor) or dimethylsulfoxide (a solvent for allopurinol) did not affect milk uric acid concentrations (P=0·96) and may indicate that heat treatment before storage and analysis was sufficient to degrade xanthine oxidase activity in milk. No relationship was observed between milk uric acid and milk yield and milk components. Authors recommend a single heat treatment (82°C for 10 min) followed by either an immediate analysis of fresh milk samples or storage at −18°C until further analysis.

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