Analyze Diet
Enzyme1988; 40(2-3); 63-69; doi: 10.1159/000469147

Structural aspects of the plasminogen of various species.

Abstract: The N-terminal amino acid sequence of equine, ovine, canine, goat and rabbit plasminogen were determined and compared with those already known of the human, bovine, porcine and feline molecule. Furthermore, the kringle 4 domains of equine, ovine, canine and goat plasminogen, prepared by limited cleavage with elastase, were sequenced and compared with the known species of human, bovine, porcine and chicken plasminogen. Homology with the human kringle 4 ranges between 73% (chicken) and 90% (bovine). Comparison of sequences, fragmentation patterns with elastase and adsorption on lysine-Bio-Gel suggests the same structural and functional domains in the animal species as in human plasminogen.
Publication Date: 1988-01-01 PubMed ID: 3168975DOI: 10.1159/000469147Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article studies the structure of plasminogen in various animal species and compares it to the human plasminogen to understand the similarities and differences.

Understanding Plasminogen and its Importance

  • Plasminogen is a vital enzyme in our blood that helps in the process of dissolving clots.
  • By studying the structure of plasminogen in different species, scientists can further their understanding of its function and how it plays a role in various biological processes.

Study of Plasminogen in Various Animals

  • The researchers first determined the N-terminal amino acid sequences of plasminogen in several animals including horses, sheep, dogs, goats, and rabbits.
  • These sequences were then compared with the already known sequences for humans, cows, pigs, and cats.

Analysis of Kringle 4 Domains

  • In addition to examining the N-terminal sequences, the scientists also studied the kringle 4 domains of the animal plasminogen.
  • Kringle 4 domains — these are specific areas of a plasminogen molecule where important biochemical interactions occur.
  • This analysis was accomplished by limited cleavage with elastase, an enzyme that can break down the plasminogen into smaller fragments.
  • The sequences of these domains were then compared with the known sequences from human, bovine, porcine, and chicken plasminogen.

Results of the Study

  • The comparison showed a significant homology (similarity) between these different species’ plasminogens and human plasminogen — ranging from 73% in chickens to 90% in cows.
  • The sequence comparisons, fragmentation analyses from elastase, and absorption data all supported the conclusion that the same structural and functional domains found in human plasminogen are also present in these animal species.

Implications of the Study

  • This research helps to expand our understanding of the structure of plasminogen and its function across different species.
  • The high level of similarity could indicate a conservation of function across various animal species, suggesting a strong evolutionary pressure to maintain these features of the plasminogen molecule.
  • Further studies could leverage these findings to investigate potential therapeutic strategies for conditions related to clotting disorders.

Cite This Article

APA
Schaller J, Rickli EE. (1988). Structural aspects of the plasminogen of various species. Enzyme, 40(2-3), 63-69. https://doi.org/10.1159/000469147

Publication

ISSN: 0013-9432
NlmUniqueID: 1262265
Country: Switzerland
Language: English
Volume: 40
Issue: 2-3
Pages: 63-69

Researcher Affiliations

Schaller, J
  • Institute of Biochemistry, University of Bern, Switzerland.
Rickli, E E

    MeSH Terms

    • Amino Acid Sequence
    • Animals
    • Cattle
    • Chickens
    • Humans
    • Molecular Sequence Data
    • Peptide Mapping
    • Plasminogen
    • Sheep
    • Species Specificity

    Citations

    This article has been cited 2 times.
    1. Wang J, Reich E. Structure and function of microplasminogen: II. Determinants of activation by urokinase and by the bacterial activator streptokinase. Protein Sci 1995 Sep;4(9):1768-79.
      doi: 10.1002/pro.5560040912pubmed: 8528075google scholar: lookup
    2. Christensen S, Sottrup-Jensen L, Christensen U. Stopped-flow fluorescence kinetics of bovine alpha 2-antiplasmin inhibition of bovine midiplasmin. Biochem J 1995 Jan 1;305 ( Pt 1)(Pt 1):97-102.
      doi: 10.1042/bj3050097pubmed: 7529997google scholar: lookup