The amino acid sequence of human myoglobin and its minor fractions

The complete amino acid sequence of human skeletal myoglobin is described. That of heart myoglobin is found by homology to be the same. When myoglobin is prepared some minor fractions may be obtained besides the main component. They are shown to be artefacts arising from deamidations. The likely thr...

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Published in:Proceedings of the Royal Society of London. Series B. Biological Sciences
Format: Article in Journal/Newspaper
Language:English
Published: The Royal Society 1974
Subjects:
Online Access:http://dx.doi.org/10.1098/rspb.1974.0048
https://royalsocietypublishing.org/doi/pdf/10.1098/rspb.1974.0048
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spelling crroyalsociety:10.1098/rspb.1974.0048 2024-06-02T08:14:52+00:00 The amino acid sequence of human myoglobin and its minor fractions 1974 http://dx.doi.org/10.1098/rspb.1974.0048 https://royalsocietypublishing.org/doi/pdf/10.1098/rspb.1974.0048 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 186, issue 1084, page 249-279 ISSN 0080-4649 2053-9193 journal-article 1974 crroyalsociety https://doi.org/10.1098/rspb.1974.0048 2024-05-07T14:16:16Z The complete amino acid sequence of human skeletal myoglobin is described. That of heart myoglobin is found by homology to be the same. When myoglobin is prepared some minor fractions may be obtained besides the main component. They are shown to be artefacts arising from deamidations. The likely three-dimensional structure of human myoglobin is discussed, taking that of sperm-whale myoglobin as a reference. Human myoglobin is compared with the α - and β -chains of human haemoglobin. There is a noteworthy similarity of internal residues and haem contacts, but little resemblance of sites where the haemoglobin chains form dimeric and tetrameric contacts, when they become subunits of the haemoglobin molecule. Article in Journal/Newspaper Sperm whale The Royal Society Proceedings of the Royal Society of London. Series B. Biological Sciences 186 1084 249 279
institution Open Polar
collection The Royal Society
op_collection_id crroyalsociety
language English
description The complete amino acid sequence of human skeletal myoglobin is described. That of heart myoglobin is found by homology to be the same. When myoglobin is prepared some minor fractions may be obtained besides the main component. They are shown to be artefacts arising from deamidations. The likely three-dimensional structure of human myoglobin is discussed, taking that of sperm-whale myoglobin as a reference. Human myoglobin is compared with the α - and β -chains of human haemoglobin. There is a noteworthy similarity of internal residues and haem contacts, but little resemblance of sites where the haemoglobin chains form dimeric and tetrameric contacts, when they become subunits of the haemoglobin molecule.
format Article in Journal/Newspaper
title The amino acid sequence of human myoglobin and its minor fractions
spellingShingle The amino acid sequence of human myoglobin and its minor fractions
title_short The amino acid sequence of human myoglobin and its minor fractions
title_full The amino acid sequence of human myoglobin and its minor fractions
title_fullStr The amino acid sequence of human myoglobin and its minor fractions
title_full_unstemmed The amino acid sequence of human myoglobin and its minor fractions
title_sort amino acid sequence of human myoglobin and its minor fractions
publisher The Royal Society
publishDate 1974
url http://dx.doi.org/10.1098/rspb.1974.0048
https://royalsocietypublishing.org/doi/pdf/10.1098/rspb.1974.0048
genre Sperm whale
genre_facet Sperm whale
op_source Proceedings of the Royal Society of London. Series B. Biological Sciences
volume 186, issue 1084, page 249-279
ISSN 0080-4649 2053-9193
op_rights https://royalsociety.org/journals/ethics-policies/data-sharing-mining/
op_doi https://doi.org/10.1098/rspb.1974.0048
container_title Proceedings of the Royal Society of London. Series B. Biological Sciences
container_volume 186
container_issue 1084
container_start_page 249
op_container_end_page 279
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