Determination of glycated hemoglobin by affinity chromatography

1987 ◽  
Vol 168 (1) ◽  
pp. 81-86 ◽  
Author(s):  
Gerhard Oremek ◽  
Ulrich B. Seiffert ◽  
Günter Schmid
Keyword(s):  
Affinity Chromatography ◽  
Glycated Hemoglobin

Quantitative Assessment of Soluble Fibrin in Plasma by Affinity Chromatography – A Comparative Study with desAA-Fibrin, desAABB-Fibrin and Fibrinogen

1985 ◽  
Vol 54 (02) ◽  
pp. 533-538 ◽  
Author(s):  
Wilfried Thiel ◽  
Ulrich Delvos ◽  
Gert Müller-Berghaus
Keyword(s):  
Affinity Chromatography ◽  
Calcium Ions ◽  
Quantitative Assessment ◽  
Fluid Phase ◽  
Soluble Fibrin ◽  
Binding Characteristics ◽  
Different Temperatures ◽  
Immobilized Proteins ◽  
Sepharose 4B

SummaryA quantitative determination of soluble fibrin in plasma was carried out by affinity chromatography. For this purpose, desAA-fibrin and fibrinogen immobilized on Sepharose 4B were used at the stationary side whereas batroxobin-induced 125I-desAA-fibrin or thrombin-induced 125I-desAABB-fibrin mixed with plasma containing 131I-fibrinogen represented the fluid phase. The binding characteristics of these mixtures to the immobilized proteins were compared at 20° C and 37° C. Complete binding of both types of fibrin to the immobilized desAA-fibrin was always seen at 20° C as well as at 37° C. However, binding of soluble fibrin was accompanied by substantial binding of fibrinogen that was more pronounced at 20° C. Striking differences depending on the temperature at which the affinity chromatography was carried out, were documented for the fibrinogen-fibrin interaction. At 20° C more than 90% of the applied desAA-fibrin was bound to the immobilized fibrinogen whereas at 37° C only a mean of 17% were retained at the fibrinogen-Sepharose column. An opposite finding with regard to the tested temperature was made with the desAABB-fibrin. Nearly complete binding to insolubilized fibrinogen was found at 37° C (95%) but only 58% of the desAABB-fibrin were bound at 20° C. The binding patterns did not change when the experiments were performed in the presence of calcium ions. The opposite behaviour of the two types of soluble fibrin to immobilized fibrinogen at the different temperatures, together with the substantial binding of fibrinogen in the presence of soluble fibrin to insolubilized fibrin in every setting tested, devaluates affinity chromatography as a tool in the quantitative assessment of soluble fibrin in patients’ plasma.

Solid-phase radioimmunoassay for morphine, with use of an affinity-purified morphine antibody.

1978 ◽  
Vol 24 (2) ◽  
pp. 339-342 ◽  
Author(s):  
M Steiner ◽  
J L Spratt
Keyword(s):  
Affinity Chromatography ◽  
Correlation Coefficient ◽  
Solid Phase ◽  
Rapid Determination ◽  
Biological Fluids ◽  
Inhibitory Effect ◽  
Major Metabolite ◽  
Solid Phase Radioimmunoassay ◽  
Related Compounds

Abstract Morphine antibody purified by affinity chromatography was used to develop a solid-phase radioimmunoassay for morphine in polystyrene tubes. The tubes are coated with an appropriate concentration of the purified antibody, rinsed three times with buffered saline, and stored at -15 degrees C. Using tritiated dihydromorphine, we determined competitive morphine binding by difference when the radioactivity in the assay supernates was measured after incubation (1 h, 37 degrees C). Five standard curves, with use of serum equivalents of morphine ranging from 0 to 6 mug/liter, were linear and had a mean correlation coefficient of 0.98. Uncer conditions of the assay, levorphanol was comparable to morphine in its inhibitory effect on binding of labeled dihydromorphine, whereas dextrorphan was essentially inactive. Morphine-3-glucuronide, a major metabolite, is 55-fold less inhibitory in terms of its capacity to displace the radiolabel. We believe that the sensitivity of the technique, coupled with the simplicity of nonseparatory sampling, renders the system suitable for rapid determination of morphine and related compounds in biological fluids.

scholarly journals Determination of serum glycated albumin by high-performance affinity chromatography.

1992 ◽  
Vol 41 (8) ◽  
pp. 387-391 ◽  
Author(s):  
Shigeru NAKATANI ◽  
Yoshio KATO ◽  
Masato NASU ◽  
Seiichi FUJITA ◽  
Yoshiaki KATAYAMA
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
Glycated Albumin ◽  
High Performance Affinity Chromatography

scholarly journals Quantification of glycated hemoglobin indicator HbA1c through near-infrared spectroscopy

2014 ◽  
Vol 07 (04) ◽  
pp. 1350060 ◽  
Author(s):  
Tao Pan ◽  
Minmiao Li ◽  
Jiemei Chen ◽  
Haiyan Xue
Keyword(s):  
Near Infrared ◽  
Glycated Hemoglobin ◽  
Correlation Coefficients ◽  
Partial Least Square ◽  
Least Square ◽  
Spectral Determination ◽  
Spectroscopic Analyses ◽  
Biochemical Indicator ◽  
New Strategy

A new strategy for quantitative analysis of a major clinical biochemical indicator called glycated hemoglobin (HbA1c) was proposed. The technique was based on the simultaneous near-infrared (NIR) spectral determination of hemoglobin (Hb) and absolute HbA1c content (Hb • HbA1c) in human hemolysate samples. Wavelength selections were accomplished using the improved moving window partial least square (MWPLS) method for stability. Each model was established using an approach based on randomness, similarity, and stability to obtain objective, stable, and practical models. The optimal wavebands obtained using MWPLS were 958 to 1036 nm for Hb and 1492 to 1858 nm for Hb • HbA1c, which were within the NIR overtone region. The validation root mean square error and validation correlation coefficients of prediction (V-SEP, V-R P ) were 3.4 g L-1 and 0.967 for Hb, respectively, whereas the corresponding values for Hb • HbA1c were 0.63 g L-1 and 0.913. The corresponding V-SEP and V-R P were 0.40% and 0.829 for the relative percentage of HbA1c. The experimental results confirm the feasibility for the quantification of HbA1c based on simultaneous NIR spectroscopic analyses of Hb and Hb • HbA1c.

Sign in / Sign up

Export Citation Format

Share Document