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Related Experiment Videos

Tris(3,5-dibromosalicyl) tricarballylate crosslinked hemoglobin: functional evaluation

Y Zheng1, K W Olsen

  • 1Department of Chemistry, Loyola University of Chicago, Chicago, IL 60626, USA.

Artificial Cells, Blood Substitutes, and Immobilization Biotechnology
|November 1, 1996
PubMed
Summary

Crosslinking human hemoglobin A with tris(3,5-dibromosalicyl) tricarballylate stabilized the protein. This crosslinking shifted hemoglobin conformation towards the R state, increasing oxygen affinity.

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Structural Biology

Background:

  • Human hemoglobin A (HbA) is crucial for oxygen transport.
  • Understanding HbA's structural dynamics is key to its function.
  • Chemical crosslinking can probe protein stability and conformation.

Purpose of the Study:

  • To investigate the effects of inter-subunit crosslinking on human hemoglobin A.
  • To analyze changes in thermal stability, autoxidation rates, and oxygen binding properties.

Main Methods:

  • Human hemoglobin A (oxy and deoxy forms) was crosslinked using tris(3,5-dibromosalicyl) tricarballylate.
  • Thermal denaturation transition temperature (Tm) was measured.
  • Autoxidation rate constants (kapp) were determined.

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  • Oxygen affinity and cooperativity were assessed.

    • Main Results:

    • The major crosslinked species contained an inter-subunit crosslink.
    • Crosslinked oxyhemoglobin Tm increased by 14.5°C; deoxyhemoglobin Tm increased by 13.0°C.
    • Deoxy crosslinked hemoglobin showed a 34% increase in autoxidation rate.
    • Crosslinked proteins exhibited higher oxygen affinity and lower cooperativity.

    Conclusions:

    • Inter-subunit crosslinking enhances hemoglobin stability.
    • The crosslink induces a conformational shift towards the R state, favoring oxygen binding.
    • Crosslinking modifies hemoglobin's functional properties, impacting oxygen transport efficiency.