Analyze Diet

[The interaction between phosphate and protein, and the respiration of the llama, the human fetus and the horse (author’s transl)].

Abstract: The sequence analysis of llama (Lama glama, Camelidae) hemoglobin is described. The chains were separated, cleaved by trypsin as previously described, quantitatively characterized and sequenced in the sequenator. The llama hemoglobin differs from the human hemoglobin in that it has 25 different amino acids in the alpha chain and 24 different amino acids in the beta chain. The interaction between protein and phosphate is discussed. The earlier finding that the O2 affinity of the llama hemoglobin is dependent on its content of 2, 3-bisphosphoglycerate is interpreted here as a mutation of the 2, 3-bisphosphoglycerate contact position beta2 His in human hemoglobin to beta2 Asn in llama hemoglobin, whereby one of the four 2, 3-bisphosphoglycerate contact points is interrupted. This interruption gives rise to a diminished reduction of intrinsic oxygen affinity in the hemoglobin molecule and explains, on a molecular basis, the increased oxygen affinity of the llama hemoglobin, and consequently, the high-altitude respiration of the llama. By analogy, the increased O2 affinity of human fetal hemoglobin is interpreted according to previous physiological investigations on blood and fetal hemoglobin by the inactivation of the phosphoglycerate contact point beta143 His in the adult hemoglobin by mutation to gamma 143 Ser in the fetal hemoglobin. With respect to respiration in horses (2, 3-bisphosphoglycerate contact beta2 Gln), measurement of atomic parameters show that the amido group of the glutamine is situated close enough to the 2, 3-bisphosphoglycerate oxygen to build a hydrogen bond with the phosphate. Consequently, the explanation of the low-altitude respiration of the horse lies in the fact that glutamine and histidine fulfill sterochemically an identical function.
Publication Date: 1978-05-01 PubMed ID: 669574
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  • Comparative Study
  • English Abstract
  • Journal Article

Summary

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This study examines the differences in oxygen-carrying hemoglobin molecules in llamas, human fetuses, and horses. The research focuses on the different amino acids in these hemoglobin molecules and how this influences respiration, particularly in the high-altitude environment inhabited by llamas.

Hemoglobin Sequencing and Analysis

  • This research detailed the separation and sequencing of llama hemoglobin, characterizing and comparing it with human hemoglobin.
  • Notably, the llama’s hemoglobin was found to contain 25 different amino acids in the alpha chain and 24 different in the beta chain, differing from human hemoglobin.

Interplay between Protein and Phosphate

  • The study takes a deeper look into interaction between protein and phosphate within the hemoglobin.
  • It brings into focus the role of 2,3-bisphosphoglycerate, a molecule that helps to regulate oxygen binding and release in hemoglobin. The level of this molecule is said to affect the oxygen affinity of llama hemoglobin.

Understanding Hemoglobin Mutations

  • The researchers interpret that the mutation of the 2,3-bisphosphoglycerate contact point in llama hemoglobin interrupts one of the four contact points this molecule has.
  • This interruption reduces the inherent oxygen affinity within the hemoglobin molecule.
  • These findings explain the molecular basis for the increased oxygen affinity of llama hemoglobin, and consequently why llamas thrive in high-altitude environments where oxygen levels are lower.

Comparison with Human Fetal and Horse Hemoglobin

  • The increased oxygen affinity in human fetal hemoglobin is also discussed, drawing parallels with earlier physiological investigations on blood and fetal hemoglobin.
  • The researchers highlight a similar mutation in human fetal hemoglobin leading to the inactivation of one of the phosphoglycerate contact points, increasing its oxygen affinity.
  • The study also looks at horse hemoglobin. It notes that the composition of the equine hemoglobin allows for formation of a hydrogen bond with the phosphate from 2,3-bisphosphoglycerate, leading to normal low-altitude respiration in horses.

Cite This Article

APA
Braunitzer G, Schrank B, Stangl A, Bauer C. (1978). [The interaction between phosphate and protein, and the respiration of the llama, the human fetus and the horse (author’s transl)]. Hoppe Seylers Z Physiol Chem, 359(5), 547-558.

Publication

ISSN: 0018-4888
NlmUniqueID: 2985060R
Country: Germany
Language: ger
Volume: 359
Issue: 5
Pages: 547-558

Researcher Affiliations

Braunitzer, G
    Schrank, B
      Stangl, A
        Bauer, C

          MeSH Terms

          • Animals
          • Camelids, New World
          • Female
          • Fetus
          • Hemoglobins
          • Horses
          • Humans
          • Oxygen / blood
          • Oxygen Consumption
          • Phosphates / blood
          • Pregnancy

          Citations

          This article has been cited 4 times.
          1. Braunitzer G. [Phosphate-hemoglobin interaction: concerning the respiration of adult man, human fetus, the llama and dromedary (author's transl)].. Klin Wochenschr 1980 Jul 15;58(14):701-8.
            doi: 10.1007/BF01478457pubmed: 7453084google scholar: lookup
          2. Liljeqvist G, Paléus S, Braunitzer G. Hemoglobins, XLVIIII. The primary structure of a monomeric hemoglobin from the hagfish, Myxine glutinosa L.: evolutionary aspects and comparative studies of the function with special reference to the heme linkage.. J Mol Evol 1982;18(2):102-8.
            doi: 10.1007/BF01810828pubmed: 7097771google scholar: lookup
          3. Jürgens KD, Pietschmann M, Yamaguchi K, Kleinschmidt T. Oxygen binding properties, capillary densities and heart weights in high altitude camelids.. J Comp Physiol B 1988;158(4):469-77.
            doi: 10.1007/BF00691144pubmed: 3220989google scholar: lookup
          4. Braunitzer G, Hiebl I. [Molecular aspects of high altitude respiration of birds. Hemoglobins of the striped goose (Anser indicus), the Andean goose, (Chloephaga melanoptera) and vulture (Gyps rueppellii)].. Naturwissenschaften 1988 Jun;75(6):280-7.
            doi: 10.1007/BF00367318pubmed: 3205309google scholar: lookup