Purification of radiolabeled monoclonal antibodies to angiotensin-converting enzyme significantly improves specificity and efficacy of its targeting into the lung

Abstract

The aim of this study was to improve the labeling/purification procedures for monoclonal antibody (MoAb) to angiotensin-converting enzyme (ACE). MoAb 9B9 was very stable upon iodination at a wide range of iodogen concentrations and incubation times, and was also very stable upon storage, indicating the high technological potential of this MoAb. Radiolabeled MoAb 9B9 was purified by (i) adsorption chromatography on cellulose, (ii) HPLC (gel filtration) and (iii) affinity chromatography on ACE-Sepharose. The best result was obtained with cellulose: specificity of MoAb 9B9 accumulation in the lung increased 2-fold. We conclude that the phenomenon of specific lung accumulation of MoAb 9B9 may serve as an ideal (convenient, cheap and technological) assay system for evaluation of monoclonal antibody modification and labeling.

Original language	English
Pages (from-to)	435-441
Number of pages	7
Journal	Nuclear Medicine and Biology
Volume	20
Issue number	4
DOIs	https://doi.org/10.1016/0969-8051(93)90074-5
Publication status	Published - 1993
Externally published	Yes

ASJC Scopus subject areas

Cancer Research
Molecular Medicine
Radiology Nuclear Medicine and imaging

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10.1016/0969-8051(93)90074-5

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Purification of radiolabeled monoclonal antibodies to angiotensin-converting enzyme significantly improves specificity and efficacy of its targeting into the lung. / Hiemisch, H.; Gavrilyuk, V.; Atochina, Elena Nikolaevna; Slinkin, M.; Torchilin, V.; Muzykantov, V.; Danilov, S.

In: Nuclear Medicine and Biology, Vol. 20, No. 4, 1993, p. 435-441.

Research output: Contribution to journal › Article › peer-review

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title = "Purification of radiolabeled monoclonal antibodies to angiotensin-converting enzyme significantly improves specificity and efficacy of its targeting into the lung",

abstract = "The aim of this study was to improve the labeling/purification procedures for monoclonal antibody (MoAb) to angiotensin-converting enzyme (ACE). MoAb 9B9 was very stable upon iodination at a wide range of iodogen concentrations and incubation times, and was also very stable upon storage, indicating the high technological potential of this MoAb. Radiolabeled MoAb 9B9 was purified by (i) adsorption chromatography on cellulose, (ii) HPLC (gel filtration) and (iii) affinity chromatography on ACE-Sepharose. The best result was obtained with cellulose: specificity of MoAb 9B9 accumulation in the lung increased 2-fold. We conclude that the phenomenon of specific lung accumulation of MoAb 9B9 may serve as an ideal (convenient, cheap and technological) assay system for evaluation of monoclonal antibody modification and labeling.",

author = "H. Hiemisch and V. Gavrilyuk and Atochina, {Elena Nikolaevna} and M. Slinkin and V. Torchilin and V. Muzykantov and S. Danilov",

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AU - Hiemisch, H.

AU - Gavrilyuk, V.

AU - Atochina, Elena Nikolaevna

AU - Slinkin, M.

AU - Torchilin, V.

AU - Muzykantov, V.

AU - Danilov, S.

PY - 1993

Y1 - 1993

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AB - The aim of this study was to improve the labeling/purification procedures for monoclonal antibody (MoAb) to angiotensin-converting enzyme (ACE). MoAb 9B9 was very stable upon iodination at a wide range of iodogen concentrations and incubation times, and was also very stable upon storage, indicating the high technological potential of this MoAb. Radiolabeled MoAb 9B9 was purified by (i) adsorption chromatography on cellulose, (ii) HPLC (gel filtration) and (iii) affinity chromatography on ACE-Sepharose. The best result was obtained with cellulose: specificity of MoAb 9B9 accumulation in the lung increased 2-fold. We conclude that the phenomenon of specific lung accumulation of MoAb 9B9 may serve as an ideal (convenient, cheap and technological) assay system for evaluation of monoclonal antibody modification and labeling.

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