Purification and properties of crustacyanin
Crustacyanin, the blue carapace pigment of the common lobster Homarus gammarus (L.), has been purified and crystallized. This chromoprotein has a minimum molecular weight of 36 000 based on the content of the carotenoid prosthetic group astaxanthin. The molecular weight in gel filtration measurement...
Published in: | Proceedings of the Royal Society of London. Series B. Biological Sciences |
---|---|
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
The Royal Society
1966
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1098/rspb.1966.0017 https://royalsocietypublishing.org/doi/pdf/10.1098/rspb.1966.0017 |
id |
crroyalsociety:10.1098/rspb.1966.0017 |
---|---|
record_format |
openpolar |
spelling |
crroyalsociety:10.1098/rspb.1966.0017 2024-06-02T08:07:51+00:00 Purification and properties of crustacyanin 1966 http://dx.doi.org/10.1098/rspb.1966.0017 https://royalsocietypublishing.org/doi/pdf/10.1098/rspb.1966.0017 en eng The Royal Society https://royalsociety.org/journals/ethics-policies/data-sharing-mining/ Proceedings of the Royal Society of London. Series B. Biological Sciences volume 164, issue 994, page 130-151 ISSN 0080-4649 2053-9193 journal-article 1966 crroyalsociety https://doi.org/10.1098/rspb.1966.0017 2024-05-07T14:16:40Z Crustacyanin, the blue carapace pigment of the common lobster Homarus gammarus (L.), has been purified and crystallized. This chromoprotein has a minimum molecular weight of 36 000 based on the content of the carotenoid prosthetic group astaxanthin. The molecular weight in gel filtration measurements is about 650 000, corresponding to some 18 molecules of astaxanthin per molecule of protein. Crustacyanin, on dialysis against water, dissociates into particles of about 35 000 molecular weight, each apparently bearing one molecule of carotenoid. The dissociation is accompanied by a shift in the principal maximum of the absorption spectrum from 633 to 595 nm and is reversed upon addition of salt. Reversible dissociation also occurs in the presence of 3 M urea, 1 M potassium thiocyanate, 10% (v/v) dioxan or 10% (v/v) acetone. When the carotenoid is removed from crustacyanin with acetone, the resultant apoprotein has a mean molecular weight of about 20 000. It may be resolved by starch gel electrophoresis into several components of which two predominate. Crustacyanin, indistinguishable from the native material, can be reconstituted from apoprotein and carotenoid. Evidence from the behaviour of crustacyanin and its apoprotein at surfaces indicates that the tertiary and quaternary structures of the native protein are stabilized by the carotenoid. It is suggested that the quaternary structure of crustacyanin is induced by an interaction of the carotenoid molecules of the subunits, which in turn causes a change in configuration of the protein favourable to aggregation. The result is a micelle-like structure with a hydrophobic carotenoid core. Article in Journal/Newspaper Homarus gammarus The Royal Society Proceedings of the Royal Society of London. Series B. Biological Sciences 164 994 130 151 |
institution |
Open Polar |
collection |
The Royal Society |
op_collection_id |
crroyalsociety |
language |
English |
description |
Crustacyanin, the blue carapace pigment of the common lobster Homarus gammarus (L.), has been purified and crystallized. This chromoprotein has a minimum molecular weight of 36 000 based on the content of the carotenoid prosthetic group astaxanthin. The molecular weight in gel filtration measurements is about 650 000, corresponding to some 18 molecules of astaxanthin per molecule of protein. Crustacyanin, on dialysis against water, dissociates into particles of about 35 000 molecular weight, each apparently bearing one molecule of carotenoid. The dissociation is accompanied by a shift in the principal maximum of the absorption spectrum from 633 to 595 nm and is reversed upon addition of salt. Reversible dissociation also occurs in the presence of 3 M urea, 1 M potassium thiocyanate, 10% (v/v) dioxan or 10% (v/v) acetone. When the carotenoid is removed from crustacyanin with acetone, the resultant apoprotein has a mean molecular weight of about 20 000. It may be resolved by starch gel electrophoresis into several components of which two predominate. Crustacyanin, indistinguishable from the native material, can be reconstituted from apoprotein and carotenoid. Evidence from the behaviour of crustacyanin and its apoprotein at surfaces indicates that the tertiary and quaternary structures of the native protein are stabilized by the carotenoid. It is suggested that the quaternary structure of crustacyanin is induced by an interaction of the carotenoid molecules of the subunits, which in turn causes a change in configuration of the protein favourable to aggregation. The result is a micelle-like structure with a hydrophobic carotenoid core. |
format |
Article in Journal/Newspaper |
title |
Purification and properties of crustacyanin |
spellingShingle |
Purification and properties of crustacyanin |
title_short |
Purification and properties of crustacyanin |
title_full |
Purification and properties of crustacyanin |
title_fullStr |
Purification and properties of crustacyanin |
title_full_unstemmed |
Purification and properties of crustacyanin |
title_sort |
purification and properties of crustacyanin |
publisher |
The Royal Society |
publishDate |
1966 |
url |
http://dx.doi.org/10.1098/rspb.1966.0017 https://royalsocietypublishing.org/doi/pdf/10.1098/rspb.1966.0017 |
genre |
Homarus gammarus |
genre_facet |
Homarus gammarus |
op_source |
Proceedings of the Royal Society of London. Series B. Biological Sciences volume 164, issue 994, page 130-151 ISSN 0080-4649 2053-9193 |
op_rights |
https://royalsociety.org/journals/ethics-policies/data-sharing-mining/ |
op_doi |
https://doi.org/10.1098/rspb.1966.0017 |
container_title |
Proceedings of the Royal Society of London. Series B. Biological Sciences |
container_volume |
164 |
container_issue |
994 |
container_start_page |
130 |
op_container_end_page |
151 |
_version_ |
1800752982536486912 |