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Title: Characterization of bromine-77-labeled proteins prepared using bromoperoxidase

Conference · · J. Nucl. Med.; (United States)
OSTI ID:7031742

The halogenating enzyme bromoperoxidase, isolated from the red algae Bonnemaisonia hamifera and Penicillus capitatus, was used to catalyze the radiohalogenation of proteins at neutral pH. Human serum albumin and canine fibrinogen were halogenated as model compounds; the proteins were labeled with Br-77, produced by the /sup 75/As(..cap alpha..,2n)/sup 77/Br reaction. For each enzyme, the essential reaction parameters (including the concentrations of hydrogen peroxide or of protein, the amount of enzyme used to catalyze the reaction, the pH of the reaction mixture, and the reaction time) were varied to obtain conditions that resulted in the highest yield of radiolabeled protein. The labeled proteins prepared with bromoperoxidase are stable with respect to loss of the radiolabel by hydrolysis and retain their biologic activity. The extension of this method to radiobromination of other types of compounds for imaging and receptor studies seems promising.

Research Organization:
Washington Univ., St. Louis, MO
OSTI ID:
7031742
Journal Information:
J. Nucl. Med.; (United States), Vol. 21:10; Conference: 28. annual meeting of the Society of Nuclear Medicine, Las Vegas, NV, USA, 16 Jun 1981
Country of Publication:
United States
Language:
English