scholarly journals Measurement of glycosylated haemoglobins and glycosylated plasma proteins in maternal and cord blood using an affinity chromatography method

Diabetologia ◽  
1983 ◽  
Vol 25 (6) ◽  
Author(s):  
P.M. Hall ◽  
G.M. Cawdell ◽  
J.G.H. Cook ◽  
B.J. Gould
Keyword(s):  
Affinity Chromatography ◽  
Cord Blood ◽  
Plasma Proteins ◽  
Chromatography Method ◽  
Glycosylated Haemoglobins

An Inexpensive, Rapid and Precise Affinity Chromatography Method for the Measurement of Glycosylated Haemoglobins

1983 ◽  
Vol 20 (3) ◽  
pp. 129-135 ◽  
Author(s):  
Pauline M Hall ◽  
J G H Cook ◽  
B J Gould
Keyword(s):  
Affinity Chromatography ◽  
Clinical Chemistry ◽  
Glycosylated Haemoglobin ◽  
Chemistry Laboratory ◽  
Chromatography Method ◽  
Clinical Chemistry Laboratory ◽  
Glycosylated Haemoglobins ◽  
Working Day ◽  
Immediate Analysis ◽  
The Cost

We have assessed an affinity chromatography technique, using commercially available materials, for the estimation of total glycosylated haemoglobin in the routine clinical chemistry laboratory. The method gives good discrimination between normals (7·31±0·92%) and diabetics (12·70±2·88%) and has excellent precision (CV 1·5-2·0%). Labile glycosylated haemoglobin is normally removed as it is so variable. There is no significant correlation between labile glycosylated haemoglobin and blood glucose. Immediate analysis of incubated haemolysates is preferable to storage of haemolysates or erythrocytes. The affinity gel can be reused about 16 times, but oxidation must be reduced by keeping the gel at 4°C in the dark when not in use. The cost of the gel is about 7p a test and 60 samples can be analysed in a working day. The method is not affected by the presence of up to 20% met-haemoglobin and should also give correct values for samples containing genetic variants of haemoglobin.

Measurement of glycosylated haemoglobins using an affinity chromatography method

1982 ◽  
Vol 125 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Barry J. Gould ◽  
Pauline M. Hall ◽  
John G.H. Cook
Keyword(s):  
Affinity Chromatography ◽  
Chromatography Method ◽  
Glycosylated Haemoglobins

Measurement of Glycosylated Haemoglobins and Glycosylated Plasma Proteins in Animal Models with Diabetes or Inappropriate Hypoglycaemia

1986 ◽  
Vol 18 (12) ◽  
pp. 795-799 ◽  
Author(s):  
B. Gould ◽  
P. Flatt ◽  
Smita Kotecha ◽  
Susan Collett ◽  
Sara Swanston-Flatt
Keyword(s):  
Animal Models ◽  
Plasma Proteins ◽  
Glycosylated Haemoglobins

scholarly journals Purification of Porcine Circovirus Type 2 Using an Affinity Chromatography Based on a Neutralizing Monoclonal Antibody against Viral Capsid Protein

Pathogens ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1564
Author(s):  
Haiqiao Bian ◽  
Chong Yu ◽  
Yanwu Wei ◽  
Li Feng ◽  
Changming Liu ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibody ◽  
Affinity Chromatography ◽  
Porcine Circovirus Type ◽  
Porcine Circovirus Type 2 ◽  
Porcine Circovirus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Chromatography Method ◽  
Viral Adsorption

Porcine circovirus type 2 (PCV2) is a DNA virus without an envelope. The viral particle is icosahedral and has a diameter of approximately 17 nm. In order to obtain the purified virus, a broad-spectrum monoclonal antibody 3A5 against PCV2 was coupled to CNBr-activated SepharoseTM 4B, and an affinity chromatography was established for PCV2 purification. A total of 6.5 mg of purified PCV2a/LG with 97% purity was obtained from 120 mL of the viral culture medium, and only PCV2 was detected by electron microscopy. No significant changes in the antigenic characteristics of the purified virus were detected by a capture enzyme-linked immunosorbent assay (ELISA). Furthermore, the titer of the purified PCV2 was 100 times higher than that of the unpurified virus. This affinity chromatography method was also used to purify PCV2b/LN590516 and PCV2d/SD446F16, and the purified viruses were detected by electron microscopy, capture ELISA, and virus titration, respectively. The results showed that these two strains can be successfully purified, but the yield is lower than that of the PCV2a strain. In addition, the purified virus could be used to study the viral adsorption and invasion of PK15 cells using indirect immunofluorescence assays. A large number of PCV2 signals were detected to transfer from the cellular surface to the periphery of the nucleus of the PK15 cells after 30 min of adsorption of the PCV2 to the PK15 cells. The affinity chromatography is a simple and convenient tool to obtain PCV2 with high purity. It could be applied for virus structure analysis, antibody preparation, and viral adsorption and invasion research.

Investigation and validation of the affinity chromatography method for measuring glycated albumin in serum and urine

1991 ◽  
Vol 202 (1-2) ◽  
pp. 11-22 ◽  
Author(s):  
Anne C. Silver ◽  
Edmund Lamb ◽  
William R. Cattell ◽  
Anne B.St.J. Dawnay
Keyword(s):  
Affinity Chromatography ◽  
Glycated Albumin ◽  
Chromatography Method ◽  
Serum And Urine

Screening the recognition properties of peptide hormone sequence mutants by analytical high performance liquid affinity chromatography on immobilized neurophysin

1988 ◽  
Vol 53 (11) ◽  
pp. 2627-2636 ◽  
Author(s):  
Giorgio Fassina ◽  
Michal Lebl ◽  
Irwin M. Chaiken
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
Peptide Hormone ◽  
Protein Recognition ◽  
Affinity Matrix ◽  
Structure Modification ◽  
Binding Properties ◽  
Chromatography Method ◽  
Contact Residues ◽  
Critical Contact

Analytical high performance liquid affinity chromatography with immobilized neurophysin was used as a molecular screen to evaluate the effects of peptide hormone structure modification on protein recognition. Immobilization of neurophysin on silica and highly cross-linked agarose occurred with retention of oxytocin and vasopressin binding properties. The effects of one-residue-at-a-time mutation, multi-site sequence simplification, and sequence randomization of critical contact residues were evaluated by extent of binding of the peptides on the affinity matrix. The analytical chromatography method also was used as a stereoselective detector to identify racemic contaminants in peptide hormone preparations.

Fibrinogen-Fibrin Interaction Studied by Affinity Chromatography

1975 ◽  
Author(s):  
A. Starnberger ◽  
H. Hörmann
Keyword(s):  
Affinity Chromatography ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Plasma Fibrinogen ◽  
Covalently Linked ◽  
Deutsche Forschungsgemeinschaft

From human plasma, fibrinogen was adsorbed at 4° C on thrombin activated immobilized fibrinogen. Additionally retained plasma proteins were eluted at 37° C with 1.0 M Trisphosphate buffer, pH 7.6. Fibrinogen was subsequently eluted with 1.0 M KBr. It was free of contaminating proteins and showed a high clottability after removing KBr. Fibrin covalently linked to Sepharose 6B was reduced with dithioerythritol in 8 M urea. Washing with 8 M urea removed only औ-chains and γ-chains, while α-chains remained fixed to the insoluble matrix. Following carboxymethylation, the affinity of the immobilized α-chains to plasma fibrinogen was tested. Fibrinogen was adsorbed as described above. This may indicate that the α-chains are predominantly responsible for fibrinogen-fibrin interaction.Supported by the Deutsche Forschungsgemeinschaft, Sonderforschungsbereich 51.

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