Skip to content
2000
Volume 3, Issue 4
  • ISSN: 1389-2037
  • E-ISSN: 1875-5550

Abstract

The exact mechanism by which four Fe-Protoporphyrin-IX (heme) moieties and four nascent globin chains combine to form human hemoglobin (α2β2) remains a mystery. Recent Soret spectral static and kinetic studies of the incorporation of CN-Hemin derivatives into an array of human globin species have provided in vitro evidence of an ordered assembly pathway, through an αheme-βglobin intermediate, that ensures correct formation of active hemoglobin tetramers.

Loading

Article metrics loading...

/content/journals/cpps/10.2174/1389203023380602
2002-08-01
2025-10-20
Loading full text...

Full text loading...

/content/journals/cpps/10.2174/1389203023380602
Loading

  • Article Type:
    Review Article
Keyword(s): aheme-bglobin; CN-Hemin derivatives; Fe-Protoporphyrin-IX; Hemoglobin
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error
Please enter a valid_number test