[Hemoglobins, XXXIII. Note on the Sequence of the hemoglobins of the horse (author’s transl)].
Abstract: The sequence analysis of the slow migrating component of the hemoglobins of horse was repeated with the automatic methode in the sequenator and the sequence of the beta-chains completed. In the alpha-chains the positions of alpha63 and alpha65 (Gly, Ala) and alpha82 and alpha85 (amides) were changed and the remaining 40 sequences of the beta-chains are reported. According to these data and biological contributions of other authors, the biological aspects of the primary structure and the polymorphism of the hemoglobins of the horse are discussed.
Publication Date: 1980-07-01 PubMed ID: 7409745
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- English Abstract
- Journal Article
Summary
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The research article focuses on studying the sequence analysis of horse hemoglobins, specifically using an automatic method to repeat the process and complete the beta-chain sequences. The study also discusses the biological implications of the primary structure and polymorphism of horse hemoglobins.
Overview of the Research
- The research focuses on the in-depth analysis of the sequence of the slow migrating component of the hemoglobins found in horses.
- The method used for this sequence analysis is an automatic process in the sequenator, a machine designed to automatically determine the sequence of proteins or peptides.
- The primary aim of the study was to complete the beta-chain sequences of horse hemoglobin.
Completion of the Beta-Chain Sequences
- The researchers also concentrated on completing the sequences of the beta-chains, which make up part of the hemoglobin molecule. These protein chains form two subunits of a hemoglobin molecule, playing a significant role in carrying oxygen to bodily tissues.
- The findings uncovered the remaining 40 sequences of the beta-chains, which were previously unknown.
Revisions in Alpha-Chains
- The study involved revisiting the alpha-chains’ arrangements and making modifications to the positions of alpha63, alpha65 (Gly, Ala) along with alpha82 and alpha85 (amides).
- These alpha chains are vital components of the hemoglobin molecule, each carrying a single molecule of oxygen to the body’s tissues.
Biological Aspects and Polymorphism
- After analyzing the sequence of the hemoglobins and completing the chains, the study discusses the biological implications of the findings.
- The primary structure of the horse hemoglobins is reflected upon, focusing on its relevance to the biological functions performed by these molecules.
- The study further explores the polymorphism of horse hemoglobins. Polymorphism refers to the occurrence of different forms, stages, or types in individual organisms or among individuals of the same species.
- The research also considers biological contributions from other authors to gain a comprehensive understanding.
Cite This Article
APA
Matsuda G, Maita T, Braunitzer G, Schrank B.
(1980).
[Hemoglobins, XXXIII. Note on the Sequence of the hemoglobins of the horse (author’s transl)].
Hoppe Seylers Z Physiol Chem, 361(7), 1107-1116.
Publication
Researcher Affiliations
MeSH Terms
- Amino Acid Sequence
- Animals
- Hemoglobins
- Horses
- Macromolecular Substances
- Peptide Fragments / analysis
- Trypsin
Citations
This article has been cited 5 times.- Zaldívar-López S, Rowell JL, Fiala EM, Zapata I, Couto CG, Alvarez CE. Comparative genomics of canine hemoglobin genes reveals primacy of beta subunit delta in adult carnivores.. BMC Genomics 2017 Feb 8;18(1):141.
- Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.. Nucleic Acids Res 1997 Sep 1;25(17):3389-402.
- Clegg JB, Goodbourn SE, Braend M. Genetic organization of the polymorphic equine alpha globin locus and sequence of the BII alpha 1 gene.. Nucleic Acids Res 1984 Oct 25;12(20):7847-58.
- Bai Y, Ueno H, Manning JM. Some factors that influence the nonenzymatic glycation of peptides and polypeptides by glyceraldehyde.. J Protein Chem 1989 Apr;8(2):299-315.
- Giardina B, Brix O, Clementi ME, Scatena R, Nicoletti B, Cicchetti R, Argentin G, Condo SG. Differences between horse and human haemoglobins in effects of organic and inorganic anions on oxygen binding.. Biochem J 1990 Mar 15;266(3):897-900.
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