Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina)
Haptoglobin (Hp) is one of the acute phase proteins (APP) in the blood of vertebrates that is involved in immune responses. Hp concentrations are found to vary under conditions of, for example, infection, trauma or cancer. These variations and the changes in its constitution are frequently used to a...
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American Chemical Society
2009
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fthzgzmk:oai:publications.hereon.de:27608 2023-06-11T04:16:00+02:00 Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) Rosenfeld, H. Lassen, S. Prange, A. 2009 https://publications.hereon.de/id/27608 https://publications.hzg.de/id/27608 en eng American Chemical Society http://dx.doi.org/10.1021/pr900035s urn:issn:1535-3893 https://publications.hereon.de/id/27608 https://publications.hzg.de/id/27608 info:eu-repo/semantics/closedAccess issn:1535-3893 Rosenfeld, H.; Lassen, S.; Prange, A.: Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina). In: Journal of Proteome Research. Vol. 8 (2009) 6, 2923 - 2932. (DOI:10.1021/pr900035s) info:eu-repo/classification/ddc/551 info:eu-repo/semantics/article Zeitschrift Artikel 2009 fthzgzmk https://doi.org/10.1021/pr900035s 2023-05-28T23:23:02Z Haptoglobin (Hp) is one of the acute phase proteins (APP) in the blood of vertebrates that is involved in immune responses. Hp concentrations are found to vary under conditions of, for example, infection, trauma or cancer. These variations and the changes in its constitution are frequently used to assess the health status of mammals. In this work, Hp from the blood plasma of diseased and healthy harbor seals was isolated and structurally characterized. The process developed for the isolation of Hp is based on glycoprotein enrichment from crude plasma samples by means of ConA lectin affinity separation. Structural features of the protein backbone and the N-glycans were determined using MALDI-TOF/TOF-MS. De novo sequencing of seal Hp revealed an α-chain composed of 84 amino acids and a β-chain comprising 245 amino acids. Comparison with Hp of the phylogenically related dog and human Hp 1−1 reveals the conserved and variable regions. All cysteine residues responsible for disulfide bonds and one glycosylation site have identical positions in the primary structures. Altogether, four possible glycosylation sites were identified. The glycoprofile is dominated by disialylated biantennary complex-type glycans. Article in Journal/Newspaper Phoca vitulina Hereon Publications (Helmholtz-Zentrum) Journal of Proteome Research 8 6 2923 2932 |
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Hereon Publications (Helmholtz-Zentrum) |
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language |
English |
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info:eu-repo/classification/ddc/551 |
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info:eu-repo/classification/ddc/551 Rosenfeld, H. Lassen, S. Prange, A. Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) |
topic_facet |
info:eu-repo/classification/ddc/551 |
description |
Haptoglobin (Hp) is one of the acute phase proteins (APP) in the blood of vertebrates that is involved in immune responses. Hp concentrations are found to vary under conditions of, for example, infection, trauma or cancer. These variations and the changes in its constitution are frequently used to assess the health status of mammals. In this work, Hp from the blood plasma of diseased and healthy harbor seals was isolated and structurally characterized. The process developed for the isolation of Hp is based on glycoprotein enrichment from crude plasma samples by means of ConA lectin affinity separation. Structural features of the protein backbone and the N-glycans were determined using MALDI-TOF/TOF-MS. De novo sequencing of seal Hp revealed an α-chain composed of 84 amino acids and a β-chain comprising 245 amino acids. Comparison with Hp of the phylogenically related dog and human Hp 1−1 reveals the conserved and variable regions. All cysteine residues responsible for disulfide bonds and one glycosylation site have identical positions in the primary structures. Altogether, four possible glycosylation sites were identified. The glycoprofile is dominated by disialylated biantennary complex-type glycans. |
format |
Article in Journal/Newspaper |
author |
Rosenfeld, H. Lassen, S. Prange, A. |
author_facet |
Rosenfeld, H. Lassen, S. Prange, A. |
author_sort |
Rosenfeld, H. |
title |
Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) |
title_short |
Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) |
title_full |
Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) |
title_fullStr |
Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) |
title_full_unstemmed |
Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina) |
title_sort |
characterization of haptoglobin in the blood plasma of harbor seals (phoca vitulina) |
publisher |
American Chemical Society |
publishDate |
2009 |
url |
https://publications.hereon.de/id/27608 https://publications.hzg.de/id/27608 |
genre |
Phoca vitulina |
genre_facet |
Phoca vitulina |
op_source |
issn:1535-3893 Rosenfeld, H.; Lassen, S.; Prange, A.: Characterization of Haptoglobin in the Blood Plasma of Harbor Seals (Phoca vitulina). In: Journal of Proteome Research. Vol. 8 (2009) 6, 2923 - 2932. (DOI:10.1021/pr900035s) |
op_relation |
http://dx.doi.org/10.1021/pr900035s urn:issn:1535-3893 https://publications.hereon.de/id/27608 https://publications.hzg.de/id/27608 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1021/pr900035s |
container_title |
Journal of Proteome Research |
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8 |
container_issue |
6 |
container_start_page |
2923 |
op_container_end_page |
2932 |
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1768373330283331584 |