Determination of Diphenylhydantoin in Human Serum by Spin Immunoassay

1975 ◽  
Vol 21 (2) ◽  
pp. 221-226 ◽  
Author(s):  
Mark R Montgomery ◽  
Jordan L Holtzman ◽  
Richard K Leute ◽  
John S Dewees ◽  
Gunner Bolz

Abstract A spin immunoassay for diphenylhydantoin is reported, which appears to give an accurate and precise estimate of serum diphenylhydantoin concentrations, as judged by the disappearance of [14C] diphenylhydantoin from the serum of a rabbIt. The assay also appears to be a reliable technique for routine diphenylhydantoin determinations, as judged from our experience with 28 patients. Serum diphenylhydantoin concentrations in the range of 1.0-50.0 mg/liter are easily determined on a 50-µl sample. Except for primidone, no significant cross reactivity was observed with eight drugs that are commonly used in conjunction with diphenylhydantoin therapy. This fast, simple, and precise method therefore appears to be readily applicable to routine determination of diphenylhydantoin.

1978 ◽  
Vol 24 (1) ◽  
pp. 155-157 ◽  
Author(s):  
W G Kramer ◽  
N L Kinnear ◽  
H K Morgan

Abstract We evaluated four commercially available 125I-digoxin radioimmunoassay kits with regard to their ability to cross react with the digoxin metabolite dehydrodigoxin. We prepared dihydrodigoxin serum samples in digoxin-free serum over the concentration range 0.4 to 5.0 microgram/liter and assayed them with each kit according to the manufacturer's instructions. The metabolite was able to displace the 125I-labeled digoxin derivative from the antibody supplied with all four kits. However, the extent of the cross reactivity depended on the kit, ranging from essentially zero to a high degree of interference. Dihydrodigoxin is the only metabolite of digoxin to have been quantitiated in human serum, and may comprise up to 30% of total glycosides. Over the clinical and therapeutic range of serum digoxin concentrations, enough dihydrodigoxin can be produced to interfere in the determination of serum digoxin concentrations by this method. We suggest that laboratories evaluate their specific kit with regard to cross reactivity to this metabolite.


Antibiotics ◽  
2018 ◽  
Vol 7 (4) ◽  
pp. 99 ◽  
Author(s):  
Anna Berlina ◽  
Anastasia Bartosh ◽  
Anatoly Zherdev ◽  
Chuanlai Xu ◽  
Boris Dzantiev

Determining antibiotic concentration in human blood provides useful pharmacokinetic information. Commonly used methods such as ELISA require a long time to obtain results and thus cannot be applied when information is needed immediately. In this study, a novel antibody-based lateral flow technique was developed for tetracycline detection in human serum. Contrary to tests developed to analyze food samples, the features of work with serum as analyzed probe were studied for the first time here. The application of labeled and unlabeled specific antibodies was compared. For this purpose, specific and anti-species antibodies were labeled with gold nanoparticles and used for antigen–antibody interaction on the membrane surface with observed staining in the test zone. For both schemes, optimal conditions were established to provide the best sensitivity. The developed assay has a limit of visual detection as low as 35 and 11 ng/mL for the direct and indirect labeled antibodies, respectively. The limit of instrumental detection is from 0.4 to 3.5 ng/mL for diluted and undiluted sera. The use of indirect antibody labeling showed a small increase in sensitivity compared to traditional direct antibody labeling. The developed method showed no cross-reactivity with antibiotics of other classes. The method was used to test samples of serum. The results showed high correlation with the data obtained by ELISA (R2 = 0.98968). The assay provides a quick assessment of the amount of antibiotics in the blood and keeps them under control throughout the duration of therapy.


Author(s):  
HJM Van Rijn ◽  
JBL Hoekstra ◽  
JHH Thijssen

Three commercially available methods for the determination of C-peptide in human serum were evaluated. All kits were found to be acceptable with respect to precision and analytical recovery, while differences were observed with respect to sensitivity and cross-reactivity to human proinsulin. Furthermore an intermethod comparison was performed. It is pointed out that, before C-peptide determination on serum from insulin-treated diabetic subjects, a PEG precipitation, to remove antibody-bound proinsulin, should be done.


1979 ◽  
Author(s):  
Daniel Walz ◽  
Thomas Brown

Human prothrombin activation is unique in that, in addition to the release of fragment 1.2 (FI.2) from the NH-terminus of prothrombin by factor Xa during the generation of thrombin, an additional 13 residue polypeptide, fragment 3 (F3), is autocatalytically removed from the amino-terminus of the thrombin A chain. We have developed a rapid radioimmunoassay for human F3 which incorporates short incubation times and the use of a preprecipitated second antibody; the assay can be performed in three hours. Specificity studies in buffer systems show prothrombin and prethrombin 1 cross-reacting at a level of 0.001; purified thrombin does not cross-react. In the presence of 5% BSA, prothrombin displays considerably less cross-reactivity. No immunoreactive material to F3 antibodies could be detected in 400 μL of plasma. Serum, obtained from whole blood clotting, contained measurable quantities of F3 (40-100 ng/mL). This amount in serum represents only 5-10% of the theoretical amount available should all of the fragment be hydrolytically cleaved during the conversion of prothrombin to thrombin. This assay procedure is currently being utilized to monitor the activation of purified human prothrombin in the absence and presence of selected plasma inhibitors. (Supported in part by NIH 05384-17 and the Michigan Heart Association).


1968 ◽  
Vol 12 ◽  
Author(s):  
R. Goossens

A precise method for the determination of the increment of the  basal area using the PressIer bore. Refering to  previous research showing that the basal area of the corsica pine could be  characterized by an ellips, we present in this paper a precise method for the  determination of the increment of the basal area. In this method we determine  the direction of the maximum diameter, we measure this diameter and we take a  core in one of the points of tangency of the caliper with the measured tree.  The determination of the diameter perpendicular to the maximum diameter  finishes the work wich is to be done in the forest. From the classical  measurements effectuated on the core and from the measured diameters we can  then determine the form (V) and the excentricity (e). Substituting these two  parameters in the formula 2 or 2', we can also calculate the error of a  radius measured on the core with respect to the representative radius, This  error with them allow us to correct the measured value of the minimum or the  maximum radius and we will be able to do a precise determination of the  increment.


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