High affinity of lead for fetal haemoglobin.

Journal Article (Journal Article)

In-vitro experiments using 203Pb were performed to identify lead-binding components in human haemoglobin. Sephadex A-50 ion-exchange chromatography of haemolysate showed that different types of haemoglobin had different affinities for lead. For the haemolysate from adults, lead was present in both Hb A (alpha 2 beta 2) and Hb A2 (alpha 2 delta 2), whereas, in the haemolysate from new-born infants, the haemoglobin of fetal origin, Hb F (alpha 2 gamma 2) showed a much greater affinity for 203Pb than the adult haemoglobin Hb A (alpha 2 beta 2), obtained from maternal blood. Analysis of the 203 Pb-labelled haemoglobin suggested that about 82% of 203Pb was in the globin polypeptide. Further analysis with carboxylmethyl (CM) cellulose chromatography indicated that the gamma globin of fetal origin had a higher affinity for 203Pb than the beta globin, whereas alpha globin appeared to be unimportant in lead binding. The results of the different affinities for lead of different Hb types are discussed with regard to the effect of lead upon haemoglobin synthesis.

Full Text

Duke Authors

Cited Authors

  • Ong, CN; Lee, WR

Published Date

  • August 1, 1980

Published In

Volume / Issue

  • 37 / 3

Start / End Page

  • 292 - 298

PubMed ID

  • 6158989

Pubmed Central ID

  • PMC1008710

International Standard Serial Number (ISSN)

  • 0007-1072

Digital Object Identifier (DOI)

  • 10.1136/oem.37.3.292


  • eng

Conference Location

  • England