ATP-HEMOGLOBIN: ANOMALOUS OXYGEN BINDING PROPERTIES

Authors
  1. McGarrity, M.J.
  2. Er, S.S.
  3. Nightingale, K.A.
  4. Hsia, J.C.
Corporate Authors
Defence and Civil Inst of Environmental Medicine, Downsview ONT (CAN)
Abstract
The results indicate that the anomalously high oxygen affinity of ATP-Hb prepared by the method of Scannon is observed simply because the bulk of the mixture is comprised of modified hemoglobins in which the triphosphate group has been lost, presumably via a beta-elimination pathway. Borohydride reduction of the imines formed o-ATP and Hb, as employed by Greenburg and Maffuid and by Hsia et al., evidently inhibits this process. It follows then that the potential of ATP-Hb as a blood substitute should not be minimized as a result of Scannon's observations. The reduced oxygen affinity of ATP-Hb and its prolonged plasma half-life make it by itself, and its polymerized derivates [i.e., poly(ATP)-Hb], potentially viable alternatives to poly(PLP)-Hb for use as hemoglobin-based blood substitutes.
Report Number
DCIEM-87-P-01 — Research Paper
Date of publication
01 Jan 1987
Number of Pages
7
Reprinted from
J of Chromatography, vol 415, 1987, p 136-142
DSTKIM No
87-02080
CANDIS No
50897
Format(s):
Hardcopy;Originator's fiche received by DSIS

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