The properties and interactions of the isolated α- and β-chains of human haemoglobin: V. The reaction of α- and β-chains

Eraldo Antonini, Enrico Bucci, Clara Fronticelli, Emilia Chiancone, Jeffries Wyman, Alessandro Rossi-Fanelli

Research output: Contribution to journalArticlepeer-review

Abstract

The mixing of the isolated α- and β-chains of human haemoglobin is accompanied by spectroscopic changes in the Soret region and by changes in the kinetics of the reaction with ligands and in sedimentation behaviour. These changes show that when the chains are combined with p-mercuribenzoate, the system is in a state of labile association—dissociation equilibrium which is strongly dependent on pH between pH 7 and 8, and is oxygen linked. The kinetics of the spectroscopic changes reveal that, both in the presence and absence of p-mercuribenzoate in the chains, the recombination is a complex process with an over-all half-time of the order of one to five seconds at 30°C, when the chains are at micromolar concentration.

Original languageEnglish (US)
Pages (from-to)29-46
Number of pages18
JournalJournal of molecular biology
Volume17
Issue number1
DOIs
StatePublished - 1966
Externally publishedYes

Keywords

  • PMB
  • p-mercuribenzoate

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint

Dive into the research topics of 'The properties and interactions of the isolated α- and β-chains of human haemoglobin: V. The reaction of α- and β-chains'. Together they form a unique fingerprint.

Cite this