Structure of arthropod hemocyanin

H. J. Bak; B. Neuteboom; P. A.  Jekel; N. M. Soeter; J. M. Vereijken; J. J.  Beintema

doi:10.1016/0014-5793(86)81402-8

Structure of arthropod hemocyanin

H. J. Bak^*, B. Neuteboom, P. A. Jekel, N. M. Soeter, J. M. Vereijken, J. J. Beintema

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map (3.2 Å resolution). Comparison of amino acid sequence data for several different hemocyanin subunits of arthropod species indicated that the general features of the polypeptide architecture as found in spiny lobster hemocyanin occur in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, 540–600 million years ago

Original language	English
Pages (from-to)	141-144
Number of pages	4
Journal	FEBS Letters
Volume	204
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(86)81402-8
Publication status	Published - 11-Aug-1986

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Structure of arthropod hemocyanin
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title = "Structure of arthropod hemocyanin",

abstract = "Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map (3.2 {\AA} resolution). Comparison of amino acid sequence data for several different hemocyanin subunits of arthropod species indicated that the general features of the polypeptide architecture as found in spiny lobster hemocyanin occur in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, 540–600 million years ago",

author = "Bak, {H. J.} and B. Neuteboom and Jekel, {P. A.} and Soeter, {N. M.} and Vereijken, {J. M.} and Beintema, {J. J.}",

year = "1986",

month = aug,

day = "11",

doi = "10.1016/0014-5793(86)81402-8",

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journal = "FEBS Letters",

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T1 - Structure of arthropod hemocyanin

AU - Bak, H. J.

AU - Neuteboom, B.

AU - Jekel, P. A.

AU - Soeter, N. M.

AU - Vereijken, J. M.

AU - Beintema, J. J.

PY - 1986/8/11

Y1 - 1986/8/11

N2 - Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map (3.2 Å resolution). Comparison of amino acid sequence data for several different hemocyanin subunits of arthropod species indicated that the general features of the polypeptide architecture as found in spiny lobster hemocyanin occur in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, 540–600 million years ago

AB - Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density map (3.2 Å resolution). Comparison of amino acid sequence data for several different hemocyanin subunits of arthropod species indicated that the general features of the polypeptide architecture as found in spiny lobster hemocyanin occur in all arthropods. This structure must therefore be at least as old as the estimated time of divergence of crustaceans and chelicerates, 540–600 million years ago

U2 - 10.1016/0014-5793(86)81402-8

DO - 10.1016/0014-5793(86)81402-8

M3 - Article

SN - 0014-5793

VL - 204

SP - 141

EP - 144

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Structure of arthropod hemocyanin

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