Literature DB >> 6653602

Radiochemical quality control of 99mTc-labelled immunoglobulin G by immobilised protein A from staphylococcus aureus.

E Sundrehagen.   

Abstract

Large fractions of immunoglobulin G (IgG) from mammalian species show high affinities for protein A isolated from staphylococcus aureus. The radiochemical purity of 99mTc-labelled IgG was determined by means of protein A, covalently bound to sepharose, by a column radiochromatographic technique and by a simpler and more rapid technique in vials. Different labelling methods produced different radiochemical purities. Limitations and applications of the testing systems are discussed.

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Year:  1983        PMID: 6653602     DOI: 10.1007/BF00252944

Source DB:  PubMed          Journal:  Eur J Nucl Med        ISSN: 0340-6997


  6 in total

1.  Electroimmuno assay.

Authors:  C B Laurell
Journal:  Scand J Clin Lab Invest Suppl       Date:  1972

2.  Reactions of staphylococcal antigens with normal sera, gamma G-globulins, and gamma G-globulin fragments of various species origin.

Authors:  A Grov; P Oeding; B Myklestad; J Aasen
Journal:  Acta Pathol Microbiol Scand B Microbiol Immunol       Date:  1970

3.  A rapid chemical method of labeling human plasma proteins with 99mTc-pertechnetate at pH 7.4.

Authors:  D W Wong; F Mishkin; T Lee
Journal:  Int J Appl Radiat Isot       Date:  1978-05

4.  Formation of 99mTc-plasmin in presence of gentisic acid using 99mTc pretreated with concentrated hydrochloric acid and vacuum evaporation.

Authors:  E Sundrehagen
Journal:  Int J Appl Radiat Isot       Date:  1982-02

5.  Formation of 99mTc-immunoglobulin G complexes free from radiocolloids, quality controlled by radioimmunoelectrophoresis.

Authors:  E Sundrehagen
Journal:  Eur J Nucl Med       Date:  1982

6.  Chemical quality control of [99mTc]plasmin by affinityradiochromatography.

Authors:  E Sundrehagen
Journal:  Int J Appl Radiat Isot       Date:  1982-12
  6 in total

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