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Biochimica et biophysica acta1977; 491(1); 265-274; doi: 10.1016/0005-2795(77)90062-9

Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice.

Abstract: Two phospholipases A2 (EC 3.1.1.4) with different isoelectric points have been isolated from horse pancreas in high yield (880 mg/kg tissue). From pancreatic juice the more acidic species was isolated as the sole phospholipase A2. Upon tryptic activation the zymogens release a hepta- and pentapeptide, respectively from the N-terminal part of the protein giving rise to the formation of one single enzyme with a specific activity higher than that of pancreatic phospholipases A2 from other mammalian species. Horse phospholipase A2 differs from the porcine and bovine enzymes with respect to amino acid composition and kinetic properties. The sequence of the first 41 amino acid residues at the N-terminus has been determined by automatic Edman degradation.
Publication Date: 1977-03-28 PubMed ID: 849461DOI: 10.1016/0005-2795(77)90062-9Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

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This study isolated two types of enzymes known as phospholipases A2 from horse pancreas in high yield, and found that these enzymes differ from similar enzymes in pigs and cows in terms of their amino acid composition and kinetic properties.

Isolation of the Phospholipases A2 Enzymes

  • Two types of enzymes, known as phospholipases A2 (EC 3.1.1.4), were obtained from horse pancreas. These enzymes were found in large quantities, with a yield of 880 milligrams per kilogram of tissue.
  • From the pancreatic juice of horses, one specific sense of this enzyme was found in isolation. The researchers referred to this kind as the “sole phospholipase A2.”

The Activation of Zymogens

  • The study also found that tryptic activation, a process in which enzymes known as trypsin stimulate the enzyme to its active form, released seven and five peptides respectively from the N-terminal part of the proteins.
  • This action led to the formation of a single enzyme with a specific activity higher than that of the same enzymes found in other mammals.

Differences between Horse Enzymes and other Species

  • The horse phospholipase A2 enzymes were found to differ from similar enzymes in pigs and cows. These differences concerned their amino acid composition and their kinetic properties, relating to the rates at which these enzymes perform their functions.
  • Through automatic Edman degradation, a technique used in protein sequencing, the researchers determined the sequence of the first 41 amino acid residues at the N-terminus of the enzymes, adding to the body of knowledge about these enzymes in horses.

Cite This Article

APA
Evenberg A, Meyer H, Verheij HM, de Haas GH. (1977). Isolation and properties of prophospholipase A2 and phospholipase A2 from horse pancreas and horse pancreatic juice. Biochim Biophys Acta, 491(1), 265-274. https://doi.org/10.1016/0005-2795(77)90062-9

Publication

ISSN: 0006-3002
NlmUniqueID: 0217513
Country: Netherlands
Language: English
Volume: 491
Issue: 1
Pages: 265-274

Researcher Affiliations

Evenberg, A
    Meyer, H
      Verheij, H M
        de Haas, G H

          MeSH Terms

          • Amino Acid Sequence
          • Amino Acids / analysis
          • Animals
          • Carbohydrates / analysis
          • Carboxypeptidases / analysis
          • Cattle
          • Disulfides / analysis
          • Horses
          • Isoenzymes / isolation & purification
          • Isoenzymes / metabolism
          • Kinetics
          • Macromolecular Substances
          • Pancreas / enzymology
          • Pancreatic Juice / enzymology
          • Phospholipases / isolation & purification
          • Phospholipases / metabolism
          • Protein Conformation
          • Species Specificity
          • Spectrophotometry, Ultraviolet
          • Swine

          Citations

          This article has been cited 3 times.
          1. Bacha AG, Mejdoub H. Proteolytic cleavage of stingray phospholipase A2: isolation and biochemical characterization of an active N-terminal form. Lipids Health Dis 2011 Jul 26;10:124.
            doi: 10.1186/1476-511X-10-124pubmed: 21791082google scholar: lookup
          2. Bacha AB, Karray A, Bouchaala E, Gargouri Y, Ali YB. Purification and biochemical characterization of pancreatic phospholipase A2 from the common stingray Dasyatis pastinaca. Lipids Health Dis 2011 Feb 17;10:32.
            doi: 10.1186/1476-511X-10-32pubmed: 21329523google scholar: lookup
          3. Karray A, Frikha F, Ben Ali Y, Gargouri Y, Bezzine S. Purification and biochemical characterization of a secreted group IIA chicken intestinal phospholipase A₂. Lipids Health Dis 2011 Feb 1;10:27.
            doi: 10.1186/1476-511X-10-27pubmed: 21284884google scholar: lookup