Authors:
G. Koželj“E. Kardelj” University Department of Chemistry and Chemical Technology, Faculty of Natural Sciences and Technology 61000 Ljubljana Yugoslavia

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B. Pihlar“E. Kardelj” University Department of Chemistry and Chemical Technology, Faculty of Natural Sciences and Technology 61000 Ljubljana Yugoslavia

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J. Marsel“E. Kardelj” University Department of Chemistry and Chemical Technology, Faculty of Natural Sciences and Technology 61000 Ljubljana Yugoslavia

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F. Gubenšek“J. Stefan” Institute Ljubljana Yugoslavia

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A. Ritonja“J. Stefan” Institute Ljubljana Yugoslavia

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I. Kregar“J. Stefan” Institute Ljubljana Yugoslavia

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Abstract  

The effect of the degree of iodination on the enzymatic activity of two enzymes, phospholipase A2 (fraction k1) and cathepsin D, was studied. The compounds were labelled with131I3 and131ICI 2 prepared by electrolysis at a controlled electrode potential. To avoid excessive denaturation of the enzyme, the electrophilic reagent was produced separately and added to the enzyme solution. Unreacted iodine species were removed by means of gel chromatography on Sephadex G-25. Enzymes were also radioiodinated by a chemical method, using chloramine T as oxidant, the results being compared with those obtained by the electrochemical method.

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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)