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 language | English |
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Pages (from-to) | 211-214 |
Number of pages | 4 |
Journal | Journal of Molecular Biology |
Volume | 111 |
Issue number | 2 |
DOIs | |
State | Published - 5 Apr 1977 |