INVITRO STABILITY AND INVIVO CLEARANCE OF FIBRINOGEN OR SERUM-ALBUMIN LABELED WITH BR-77, I-131, OR I125 BY DIRECT OR INDIRECT SYNTHETIC METHODS

  • 1 January 1977
    • journal article
    • research article
    • Vol. 18  (3) , 282-288
Abstract
Conventional protein iodination involves the addition of an oxidizing agent to the protein solution. Through the use of the acylating agent N-succinimidyl-3(4-hydroxyphenyl)propionate, labeling can be accomplished without subjecting the protein to oxidizing conditions. Fibrinogen [rabbit, dog] and serum albumin [human] labeled with 131I and 77Br by this technique were compared with each other and with 125I-protein prepared by direct iodination using the ICl, chloramine-T and lactoperoxidase methods. Iodinated proteins have 2 drawbacks: the high radiation dose accompanying 125I and 131I, and the ease of hydrolysis of the weak C-I bond. These drawbacks can be overcome by using 56-h 77Br.

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