Evaluation of four assay methods for determination of tobramycin in human serum.

Abstract Four assay procedures for tobramycin in serum--enzyme immunoassay (I), substrate-labeled fluorescent immunoassay (II), radioimmunoassay (III), and bioassay (IV)--were compared and evaluated by replicate and analytical recovery studies. I and II were about 50% more precise than III and IV. II was substantially more nearly accurate than the other methods and also gave the best reproducibility (correlation coefficient 0.992 between-day). The least expensive method was IV. Ease of handling favored I and II. Overall, we find II to be the most acceptable procedure for use in the clinical laboratory.

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Chemical assay, involving liquid chromatography, for aminoglycoside antibiotics in serum.

Clinical Chemistry ◽

10.1093/clinchem/25.7.1222 ◽

1979 ◽

Vol 25 (7) ◽

pp. 1222-1225 ◽

Cited By ~ 23

Author(s):

S E Bäck ◽

I Nilsson-Ehle ◽

P Nilsson-Ehle

Keyword(s):

Liquid Chromatography ◽

Serum Proteins ◽

Clinical Laboratory ◽

Reversed Phase ◽

Chemical Assay ◽

Analytical Recovery ◽

On Line ◽

Assay Methods ◽

Routine Clinical Laboratory

Abstract We describe a chemical assay involving "high-pressure" liquid chromatography for the quantitative determination of three aminoglycosides: netilmicin, tobramycin, and gentamicin. The drugs are separated from serum by means of precipitation of the serum proteins with acetonitrile after dilution with a buffer. The aminoglycosides are quantitatively extracted into the supernate, which is further purified by a two-step partition procedure involving derivatization of the drugs with o-phthalaldehyde. The drug derivatives are separated by reversed-phase chromatography and detected by on-line fluorometry. Sensitivity is 1 mg/L for tobramycin and 0.5 mg/L for netilmicin and gentamicin. Intra- and interassay variation was below 8%. Analytical recovery of each of the three drugs was 92 to 100%. Correlation with microbiological and radioimmunological assay methods was good. The assay is rapid (about 30 min), precise, and specific, and seems suitable for use in a routine clinical laboratory.

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Determination of thyroxine-binding globulin in human serum by single radial immunodiffusion and radioimmunoassay.

Clinical Chemistry ◽

10.1093/clinchem/23.9.1694 ◽

1977 ◽

Vol 23 (9) ◽

pp. 1694-1699 ◽

Cited By ~ 14

Author(s):

B Kågedal ◽

M Källberg

Keyword(s):

Human Serum ◽

Reference Values ◽

The Other ◽

Radial Immunodiffusion ◽

Good Precision ◽

Acylating Agent ◽

Thyroxine Binding Globulin ◽

Analytical Recovery ◽

Monospecific Antiserum

Abstract Two immunochemical methods for determination of thyroxine-binding globulin in human serum were developed, in which the purified globulin and monospecific antiserum to it are used. One method, based on radial immunodiffusion, has good precision and values for analytical recovery. Reference values obtained for men were 9.8-17.8 mg/liter and for women 11.3-20.5 mg/liter. The sex-related difference was significant. The other method is based on radioimmunoassay, with use of an iodinated acylating agent for the labeling of thyroxine-binding globulin. The relative merits of the two methods are discussed.

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Varieties of Human Serum Lipoprotein Pattern: Evaluation by Agarose Gel Electrophoresis

Clinical Chemistry ◽

10.1093/clinchem/17.5.427 ◽

1971 ◽

Vol 17 (5) ◽

pp. 427-429 ◽

Cited By ~ 8

Author(s):

N M Papadopoulos ◽

J A Kintzios

Keyword(s):

Human Serum ◽

Gel Electrophoresis ◽

Clinical Laboratory ◽

Serum Lipoprotein ◽

Agarose Gel ◽

Agarose Gel Electrophoresis ◽

Practical Applications ◽

Electrophoretic Technique ◽

Lipoprotein Pattern

Abstract A previously reported agarose gel electrophoretic technique for the determination of serum lipoprotein patterns has been modified for analysis of a large number of samples for screening and epidemiological purposes. In addition, we demonstrate the varieties of lipoprotein patterns that can clearly be distinguished and visually evaluated for practical applications in the clinical laboratory.

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Microplate Chemiluminescence Enzyme Immunoassay for the Determination of Carcinoembryonic Antigen in Human Serum

Chinese Journal of Analytical Chemistry ◽

10.1016/s1872-2040(08)60058-4 ◽

2008 ◽

Vol 36 (8) ◽

pp. 1056-1060 ◽

Cited By ~ 4

Author(s):

Tian-Bing XIN ◽

Xu WANG ◽

Hui JIN ◽

Jing-Hui CHE ◽

Shu-Xuan LIANG ◽

...

Keyword(s):

Human Serum ◽

Carcinoembryonic Antigen ◽

Enzyme Immunoassay ◽

Chemiluminescence Enzyme Immunoassay

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Evaluation of a commercial enzyme immunoassay for insulin in human serum, and its clinical application.

Clinical Chemistry ◽

10.1093/clinchem/25.1.35 ◽

1979 ◽

Vol 25 (1) ◽

pp. 35-38 ◽

Cited By ~ 13

Author(s):

M Yoshioka ◽

H Taniguchi ◽

A Kawaguchi ◽

T Kobayashi ◽

K Murakami ◽

...

Keyword(s):

Human Serum ◽

Enzyme Immunoassay ◽

Clinical Laboratory ◽

Reduced Glutathione ◽

Serum Insulin ◽

Aminosalicylic Acid ◽

Hydrogen Donors ◽

Sandwich Method ◽

High Concentrations ◽

Commercial Enzyme Immunoassay

Abstract We applied a "sandwich" method, with use of beads coated with anti-insulin serum and of peroxidase-labeled anti-insulin serum, to an enzyme immunoassay of insulin in human serum. 5-Aminosalicylic acid was used as the substrate for the enzymic reaction. As little as 5 milli-int. units of insulin per liter of serum insulin was detectable. Reproducibility was satisfactory, but extraordinarily high concentrations of proinsulin and of hydrogen donors such as reduced glutathione affect results of the assay. Values determined by our enzyme immunoassay and by double-antibody radioimmunoassay correlated highly (r = 0.938, p less than 0.001, n = 216). We recommend this method for use in the clinical laboratory.

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Specific immunoassay of alpha-amylase isoenzymes in human serum.

Clinical Chemistry ◽

10.1093/clinchem/31.8.1331 ◽

1985 ◽

Vol 31 (8) ◽

pp. 1331-1334 ◽

Cited By ~ 23

Author(s):

M Gerber ◽

K Naujoks ◽

H Lenz ◽

W Gerhardt ◽

K Wulff

Keyword(s):

Monoclonal Antibody ◽

Human Serum ◽

Enzyme Immunoassay ◽

Amylase Activity ◽

Alpha Amylase ◽

Pancreatic Amylase ◽

Routine Method ◽

Salivary Amylase ◽

Amylase Isoenzymes

Abstract A monoclonal antibody (66C7) was prepared that specifically binds human salivary amylase (EC 3.2.1.1); it cross reacts with human pancreatic amylase by less than 1%. Two procedures are described for determination of isoamylases in human serum with this antibody: an enzyme immunoassay for determining amylase of salivary origin, and a routine method in which this amylase is immunoprecipitated and the remaining (pancreatic) amylase activity is assayed. Results by the two methods correlate well.

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