Experimental basis of standardized specimen collection: The effect of moderate ethanol consumption on some serum components (K, Na, ASAT, ALAT, CK, LD, total protein)

1987 ◽  
Vol 47 (4) ◽  
pp. 337-343 ◽  
Author(s):  
E. A. Leppanen ◽  
R. Grasbeck
Keyword(s):  
Total Protein ◽  
Ethanol Consumption ◽  
Experimental Basis ◽  
Specimen Collection ◽  
Serum Components

Hemoglobin interference from in vivo hemolysis.

1985 ◽  
Vol 31 (9) ◽  
pp. 1566-1569 ◽  
Author(s):  
D W Blank ◽  
M H Kroll ◽  
M E Ruddel ◽  
R J Elin
Keyword(s):  
Lactate Dehydrogenase ◽  
Total Protein ◽  
Intravascular Hemolysis ◽  
Serum Samples ◽  
Lactate Dehydrogenase Activity ◽  
Specimen Collection ◽  
Potassium Lactate

Abstract Laboratory values for specimens from a case of intravascular hemolysis showed that hemoglobin was significantly increased and thus could interfere with the determination of other analytes. We studied this problem by adding increasing amounts of purified hemoglobin (to a maximum concentration of 19.3 mg/L) to aliquots of pooled serum samples. The hemoglobin significantly interfered with the determination of only five analytes: albumin, aspartate aminotransferase, direct bilirubin, and total protein on the SMAC, and creatinine on the Astra. We propose that for cases of proven intravascular hemolysis, values for only the analytes not affected by hemoglobin should be reported. We find lactate dehydrogenase activity useful in assessing the components of in vivo hemolysis; the differences between serum and plasma values for potassium, lactate dehydrogenase, and hemoglobin are related to in vitro hemolysis. Criteria for specimen collection and assessment of type of hemolysis are proposed.

Specimen Collection Effect in Scanning Electron Microscopy Images

1972 ◽  
Vol 30 ◽  
pp. 448-449
Author(s):  
J. Temple Black ◽  
Jose Guerrero
Keyword(s):  
Surface Morphology ◽  
Secondary Electron Emission ◽  
Secondary Electrons ◽  
Charge Effects ◽  
Material Density ◽  
Specimen Collection ◽  
The Subject ◽  
Curved Paths ◽  
Subject Material ◽  
Microscopy Images

In the SEM, contrast in the image is the result of variations in the volume secondary electron emission and backscatter emission which reaches the detector and serves to intensity modulate the signal for the CRT's. This emission is a function of the accelerating potential, material density, chemistry, crystallography, local charge effects, surface morphology and especially the angle of the incident electron beam with the particular surface site. Aside from the influence of object inclination, the surface morphology is the most important feature In producing contrast. “Specimen collection“ is the name given the shielding of the collector by adjacent parts of the specimen, producing much image contrast. This type of contrast can occur for both secondary and backscatter electrons even though the secondary electrons take curved paths to the detector-collector.Figure 1 demonstrates, in a unique and striking fashion, the specimen collection effect. The subject material here is Armco Iron, 99.85% purity, which was spark machined.

Autoantibodies to Thrombomodulin: Development of an Enzyme Immunoassay and a Survey of their Frequency in Patients with the Lupus Anticoagulant

1992 ◽  
Vol 67 (05) ◽  
pp. 507-509 ◽  
Author(s):  
John Gibson ◽  
Margaret Nelson ◽  
Ross Brown ◽  
Hatem Salem ◽  
Harry Kronenberg
Keyword(s):  
Enzyme Immunoassay ◽  
Lupus Anticoagulant ◽  
Specific Binding ◽  
Technical Problem ◽  
Serum Samples ◽  
Citrate Buffer ◽  
The Mean ◽  
Sample Dilution ◽  
Negative Population ◽  
Serum Components

SummaryIn order to investigate the possibility that autoantibodies to thrombomodulin (TM) may exist in patients with the lupus anticoagulant (LA) and perhaps be implicated in the pathogenesis of recurrent thrombosis seen in such patients, we developed an enzyme-immunoassay to screen serum samples for anti-human TM activity. The major technical problem encountered in developing this assay was to reduce the non-specific binding of serum components from both the LA positive and the negative population. Considerable reduction of non-specific binding was achieved by use of a phosphate/citrate buffer at pH 8.0 and the use of an optimal sample dilution of 1/40. In addition, samples were always tested in parallel in blank wells and results are expressed as an OD ratio. Samples from 113 patients with the LA were assayed and compared to 78 patients referred for LA testing but found to be negative. The mean OD values for the LA positive patients (± SD) was 1.36 (0.44) with a range of 0.78-2.57. This was virtually identical to the values for the LA negative population (1.38 ± 0.40, range 0.76-2.77). The results of this study indicate that there is no evidence for the presence of a significant autoantibody activity to TM in patients with the LA when compared to LA negative patients. If such autoantibodies do exist their frequency must be quite low.

A Mutation in the Protein S Pseudogene Is Linked to Protein S Deficiency in a Thrombophilic Family

1989 ◽  
Vol 62 (03) ◽  
pp. 897-901 ◽  
Author(s):  
Hans K Ploos van Amstel ◽  
Pieter H Reitsma ◽  
Karly Hamulyák ◽  
Christine E M de Die-Smulders ◽  
Pier M Mannucci ◽  
...  
Keyword(s):  
Total Protein ◽  
Protein S ◽  
Southern Analysis ◽  
Type I ◽  
Protein S Deficiency ◽  
S Deficiency ◽  
The Family ◽  
Dna Pattern ◽  
Deficiency Type ◽  
S Genes

SummaryProbands from 15 unrelated families with hereditary protein S deficiency type I, that is having a plasma total protein S concentration fifty percent of normal, were screened for abnormalities in their protein S genes by Southern analysis. Two probands were found to have a deviating DNA pattern with the restriction enzyme Mspl. In the two patients the alteration concerned the disappearance of a Mspl restriction site, CCGG, giving rise to an additional hybridizing Mspl fragment.Analysis of relatives of both probands showed that in one family the mutation does not co-segregate with the phenotype of reduced plasma protein S. In the family of the other proband, however, complete linkage between the mutated gene pattern and the reduced total protein S concentration was found: 12 heterozygous relatives showed the additional Mspl fragment but none of the investigated 26 normal members of the family. The mutation is shown to reside in the PSβ gene, the inactive protein S gene. The cause of type I protein S deficiency, a defect PSα gene has escaped detection by Southern analysis. No recombination has occurred between the PSα gene and the PSβ gene in 23 informative meioses. This suggests that the two protein S genes, located near the centromere of chromosome 3, are within 4 centiMorgan of each other.

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