Subunit structure of hemoglobin from the clam shrimp Cyzicus

Melvyn M. David*, Abel Schejter, Ezra Daniel, Yehuda Ben-Shaul

*Corresponding author for this work

Research output: Contribution to journalLetterpeer-review

11 Scopus citations

Abstract

The subunit structure of hemoglobin from the clam shrimp Cyzicus was investigated. The native protein has a molecular weight of 280,000 as shown by sedimentation equilibrium. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the presence of mercaptoethanol resulted in a single band corresponding to a molecular weight of 15,500. A molecular weight of 14,500 was determined by the method of sedimentation equilibrium for the isolated polypeptide chain. Electron microscopy of the protein revealed a pentagonal structure. It was concluded that the native molecule contains 20 polypeptide chains.

Original languageEnglish
Pages (from-to)211-214
Number of pages4
JournalJournal of Molecular Biology
Volume111
Issue number2
DOIs
StatePublished - 5 Apr 1977

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