Authors:
Y. M. Efimova Department of Radiochemistry, Delft University of Technology Mekelweg 15, 2629 JB Delft, The Netherlands

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B. Wierczinski Department of Radiochemistry, Delft University of Technology Mekelweg 15, 2629 JB Delft, The Netherlands

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S. Haemers Department of Radiochemistry, Delft University of Technology Mekelweg 15, 2629 JB Delft, The Netherlands

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A. A. van Well Department of Neutron Scattering and Mössbauer Spectroscopy, Interfaculty Reactor Institute, Delft University of Technology Mekelweg 15, 2629 JB Delft, The Netherlands

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Summary  

Bovine serum albumin (BSA) and lysozyme (LSZ) were radiolabeled with 125I. Three different methods for protein iodination with 125I were optimized. Parameters like incubation time and ratio of oxidizing agent and amount of protein were established. During protein iodination with 125I, structural damages caused by the introduction of iodine into the protein may occur. These damages depend on the oxidizing agent used and may lead to considerable changes in the protein structure and, hence, their biological activity. Changes in secondary structure of LSZ and BSA were examined by circular dichroism (CD). Enzymatic activity tests were performed with lysozyme to check its biological activity. The Iodo Bead was found the best oxidizing agent for protein iodination.

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Journal of Radionalytical and Nuclear Chemistry
Language English
Size A4
Year of
Foundation
1968
Volumes
per Year
1
Issues
per Year
12
Founder Akadémiai Kiadó
Founder's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address
H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher
Chief Executive Officer, Akadémiai Kiadó
ISSN 0236-5731 (Print)
ISSN 1588-2780 (Online)