Comparative Structural and Immunochemical Properties of Leghaemoglobins
Circular dichroism studies on leghaemoglobins from snake bean, lupin, serradella and other plants show that, in common with soybean (reported earlier) they have a similar overall polypeptide chain conformation and haem environment and orientation. Immunochemical studies, on the other hand, suggest t...
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crwiley:10.1111/j.1432-1033.1976.tb10528.x 2024-06-02T08:14:54+00:00 Comparative Structural and Immunochemical Properties of Leghaemoglobins HURRELL, John G. R. NICOLA, Nicos A. BROUGHTON, William J. DILWORTH, Michael J. MINASIAN, Elizabeth LEACH, Sydney J. 1976 http://dx.doi.org/10.1111/j.1432-1033.1976.tb10528.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1976.tb10528.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1976.tb10528.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Biochemistry volume 66, issue 2, page 389-399 ISSN 0014-2956 1432-1033 journal-article 1976 crwiley https://doi.org/10.1111/j.1432-1033.1976.tb10528.x 2024-05-03T10:40:30Z Circular dichroism studies on leghaemoglobins from snake bean, lupin, serradella and other plants show that, in common with soybean (reported earlier) they have a similar overall polypeptide chain conformation and haem environment and orientation. Immunochemical studies, on the other hand, suggest that the antigenic determinants on the surface of the leghaemoglobins vary considerably. Thus, firstly the α‐helix content of the leghaemoglobins as a class is very similar (60–65%) and approaches that of the myoglobins, secondly, the sign, magnitude and shape of their circular dichroism spectra in the near ultraviolet, Soret and visible regions suggest close similarities in the environment and orientation of a structurally important tryptophan residue and of the haem moiety, and thirdly, there is comparatively weak haem‐protein interaction. The extent of immuno cross‐reactivity was found to be best demonstrated using the Farr radioimmunoassay procedure. The results were (a) 5 leghaemoglobins from one plant (soybean) crossreacted completely but with varying affinities. (b) The extent of cross reactivity between leghaemoglobins from different plants was compared to that within a single plant; the reaction of antiserum to a soybean leghaemoglobin with a serradella leghaemoglobin was weak, with a snake bean leghaemoglobin still weaker (and incomplete) while lupin leghaemoglobins showed no cross reactivity at all. (c) The “rapid” attenuation of cross reactivity among different plant leghaemoglobins is explicable in terms of the extensive amino acid substitutions which have been demonstrated in the literature and in the present studies. (d) In view of this rapid divergence it is not surprising that sperm whale and horse heart myoglobins showed no cross reactivity with soybean leghaemoglobins. In summary, amino acid substitutions in the leghaemoglobin family are conformationally but not immunochemically conservative. Article in Journal/Newspaper Sperm whale Wiley Online Library European Journal of Biochemistry 66 2 389 399 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Circular dichroism studies on leghaemoglobins from snake bean, lupin, serradella and other plants show that, in common with soybean (reported earlier) they have a similar overall polypeptide chain conformation and haem environment and orientation. Immunochemical studies, on the other hand, suggest that the antigenic determinants on the surface of the leghaemoglobins vary considerably. Thus, firstly the α‐helix content of the leghaemoglobins as a class is very similar (60–65%) and approaches that of the myoglobins, secondly, the sign, magnitude and shape of their circular dichroism spectra in the near ultraviolet, Soret and visible regions suggest close similarities in the environment and orientation of a structurally important tryptophan residue and of the haem moiety, and thirdly, there is comparatively weak haem‐protein interaction. The extent of immuno cross‐reactivity was found to be best demonstrated using the Farr radioimmunoassay procedure. The results were (a) 5 leghaemoglobins from one plant (soybean) crossreacted completely but with varying affinities. (b) The extent of cross reactivity between leghaemoglobins from different plants was compared to that within a single plant; the reaction of antiserum to a soybean leghaemoglobin with a serradella leghaemoglobin was weak, with a snake bean leghaemoglobin still weaker (and incomplete) while lupin leghaemoglobins showed no cross reactivity at all. (c) The “rapid” attenuation of cross reactivity among different plant leghaemoglobins is explicable in terms of the extensive amino acid substitutions which have been demonstrated in the literature and in the present studies. (d) In view of this rapid divergence it is not surprising that sperm whale and horse heart myoglobins showed no cross reactivity with soybean leghaemoglobins. In summary, amino acid substitutions in the leghaemoglobin family are conformationally but not immunochemically conservative. |
format |
Article in Journal/Newspaper |
author |
HURRELL, John G. R. NICOLA, Nicos A. BROUGHTON, William J. DILWORTH, Michael J. MINASIAN, Elizabeth LEACH, Sydney J. |
spellingShingle |
HURRELL, John G. R. NICOLA, Nicos A. BROUGHTON, William J. DILWORTH, Michael J. MINASIAN, Elizabeth LEACH, Sydney J. Comparative Structural and Immunochemical Properties of Leghaemoglobins |
author_facet |
HURRELL, John G. R. NICOLA, Nicos A. BROUGHTON, William J. DILWORTH, Michael J. MINASIAN, Elizabeth LEACH, Sydney J. |
author_sort |
HURRELL, John G. R. |
title |
Comparative Structural and Immunochemical Properties of Leghaemoglobins |
title_short |
Comparative Structural and Immunochemical Properties of Leghaemoglobins |
title_full |
Comparative Structural and Immunochemical Properties of Leghaemoglobins |
title_fullStr |
Comparative Structural and Immunochemical Properties of Leghaemoglobins |
title_full_unstemmed |
Comparative Structural and Immunochemical Properties of Leghaemoglobins |
title_sort |
comparative structural and immunochemical properties of leghaemoglobins |
publisher |
Wiley |
publishDate |
1976 |
url |
http://dx.doi.org/10.1111/j.1432-1033.1976.tb10528.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1976.tb10528.x https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1976.tb10528.x |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
European Journal of Biochemistry volume 66, issue 2, page 389-399 ISSN 0014-2956 1432-1033 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1432-1033.1976.tb10528.x |
container_title |
European Journal of Biochemistry |
container_volume |
66 |
container_issue |
2 |
container_start_page |
389 |
op_container_end_page |
399 |
_version_ |
1800738906393542656 |