Bimane fluorescent labels. Characterization of the bimane labeling of human hemoglobin

Nechama S. Kosower*, Gerald L. Newton, Edward M. Kosower, Helen M. Ranney

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

60 Scopus citations


The products of the bimane labeling (using a monobromobimane, a dibromobimane and a quaternary bromobimane) of hemoglobin are characterized. Peptide mapping identifies cysteine-β93 as the reactive thiol site. Electrophoretic mobility of hemoglobin varies with the label used, that of monobromobimane-labeled hemoglobin being unaltered, while dibromobimane- and trimethylammoniobromobimane-labeled hemoglobin exhibit changes. The oxygen affinity of labeled hemoglobin is changed from that of hemoglobin. Deoxyhemoglobin is subtantially less reactive towards monobromobimane than oxyhemoglobin. Bimane-labeled hemoglobin is more easily denatured on heating than unlabeled hemoglobin. Possible uses for bimane labels in the study of protein properties are pointed out. Bimane labeling agents are derivatives of 3,4,6,7-tetramethyl-l,5-diazabicyclo[3.3.0]-octa-3,6-diene-2,8.dione 9,10-dioxa-syn-(methyl,methyl)bimane).

Original languageEnglish
Pages (from-to)201-209
Number of pages9
JournalBBA - Protein Structure
Issue number2
StatePublished - 25 Apr 1980
Externally publishedYes


  • Bimane labeling
  • Electrophoretic mobility
  • Hemoglobin
  • Oxygen affinity


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