Subunit structure of hemoglobin from the clam shrimp Cyzicus

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

doi:10.1016/S0022-2836(77)80125-3

Subunit structure of hemoglobin from the clam shrimp Cyzicus

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

^*Corresponding author for this work

Biochemistry Molecular Biology

Research output: Contribution to journal › Letter › peer-review

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
Pages (from-to)	211-214
Number of pages	4
Journal	Journal of Molecular Biology
Volume	111
Issue number	2
DOIs	https://doi.org/10.1016/S0022-2836(77)80125-3
State	Published - 5 Apr 1977

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title = "Subunit structure of hemoglobin from the clam shrimp Cyzicus",

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.",

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AU - Schejter, Abel

AU - Daniel, Ezra

AU - Ben-Shaul, Yehuda

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Y1 - 1977/4/5

N2 - 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.

AB - 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.

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U2 - 10.1016/S0022-2836(77)80125-3

DO - 10.1016/S0022-2836(77)80125-3

M3 - מזכר

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SP - 211

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 2

ER -

Subunit structure of hemoglobin from the clam shrimp Cyzicus

Abstract

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