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Journal ArticleDOI

Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobins

J. Rousseaux, +2 more
- 19 Jul 1976 - 
- Vol. 439, Iss: 1, pp 55-62
TLDR
Comparison with other ungulates shows that pig myoglobin is far from other artiodactyls previously studied and close to the eutherian ancestral chain.
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This article is published in Biochimica et Biophysica Acta.The article was published on 1976-07-19. It has received 28 citations till now. The article focuses on the topics: Globin & Myoglobin.

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Citations
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Journal ArticleDOI

Fitting the Gene Lineage into its Species Lineage, a Parsimony Strategy Illustrated by Cladograms Constructed from Globin Sequences

TL;DR: In this article, it was shown that the gene lineages deviate relatively little from established species relationships, and that most contemporary gene pairs in this phylogenetic system may be regarded as orthologous rather than paralogous (split at the time of speciation) rather than split prior to speciation, and it also appeared that as the statistical sample of orthologyous sequence sites becomes greatly enlarged by tandem alignment of enough different types of protein chains, the parsimony reconstruction based strictly on minimal nucleotide replacement length will itself reveal the correct cladogram for the set of contemporary species
Journal ArticleDOI

Myoglobin chemistry and meat color.

TL;DR: An overview of the current research in meat color and how the findings are applied in the meat industry is provided to help engineer innovative processing strategies to minimize meat discoloration-induced revenue loss to the agricultural economy.
Journal ArticleDOI

Proteomics of lipid oxidation-induced oxidation of porcine and bovine oxymyoglobins

TL;DR: Quantitation of HNE‐adducted peptides using isotope‐labeled phenyl isocyanate indicated that, initially, HIS 36 was preferentially adducted in porcine Mb whereas HIS 81, 88 and 93 were the predominant sites of early HNE adduction in bovine Mb, which may explain why lipid oxidation‐induced OxyMb oxidation appears more extensive in beef, than in pork.
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Effect of high pressure treatment on the color of fresh and processed meats: A review.

TL;DR: The pressure-induced color changes in meat are discussed in relation to modification of the myoglobin molecule, changes in the meat microstructure, and the impact of the presence of different chemical compounds and physical conditions during processing.
Journal ArticleDOI

Characterization of bison (Bison bison) myoglobin.

TL;DR: The present study is the first to report the primary structure of bison Mb, a alternate meat species gaining increased popularity in North America, which suggested that the observed rapid discoloration in bison meat could not be attributed to biochemistry of bisons Mb.
References
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Journal ArticleDOI

Strategy and tactics in protein chemistry.

B S Hartley
- 01 Oct 1970 - 
Journal ArticleDOI

Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8 Å Resolution: The Atomic Model

TL;DR: The structure of the contacts between unlike subunits suggests that the tetramer, rather than the αβ dimer, is the functional unit of haemoglobin.
Journal ArticleDOI

Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups.

TL;DR: Electrophoretic Mobilities of Peptides on Paper and their Use in the Determination of Amide Groups and their use in the determination of amide groups are studied.
Journal ArticleDOI

Micropolyamide thin-layer chromatography of phenylthiohydantoin amino acids (PTH) at subnanomolar level. A rapid microtechnique for simultaneous multisample identification after automated Edman degradations.

TL;DR: A tlc-technique for two-dimensional separation of 24 most common PTH 1 -amino acids obtained after manual or automated Edman degradations is developed and in addition to direct Edman degradation allows correct placing of Gln and Asn within sequences.
Journal ArticleDOI

Molecular Evolution of Myoglobin and the Fossil Record: a Phylogenetic Synthesis

TL;DR: An ancestral myoglobin chain has been deduced by comparing the differences in the amino acid sequences of eighteen living species and assessing from the fossil evidence the probable times of divergence of their ancestors.
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