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Amino acid sequence of phospholipase A2 from horse pancreas.
Abstract: The complete amino acid sequence of phosphlipase A2 (EC 3.1.1.4) from horse pancreas was determined. The protein controls of a single polypeptide chain of 125 amino acids and has a molecular weight of 13,927. The chain is crosslinked by seven disulfide bridges. The sequence was determined by automated Edman degradation of the intact protein and several of the large peptide fragments. Smaller peptides were analyzed by manual Edman degradation. Fragmentation of the peptide chain was accomplished by enzymatic digestion with trypsin, chymotrypsin, and thermolysin. The final overlap was found by digestion of the polypeptide with a staphylococcal protease specific for glutamoyl bonds. Phospholipase A2 from horse pancreas shows homology to snake venom phospholipases A2 and to the enzyme from porcine pancreas, provided that the published amino acid sequence of the porcine phospholipase A2 is revised to some extent.
Publication Date: 1977-02-25 PubMed ID: 838712 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
Summary
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This study presents the complete amino acid sequence of phosphlipase A2, an enzyme from horse pancreas. This enzyme is made up of a single chain of 125 amino acids, and is related in structure to similar enzymes in snake venom and pig pancreas.
Objective and Methodology
- The research aimed at determining the complete amino acid sequence of phosphlipase A2 from the horse pancreas. The protein is composed of a single polypeptide chain of 125 amino acids with a molecular weight of 13,927. The protein chain is held together by seven disulfide bridges.
- The sequence determination was done by automated Edman degradation, a process of sequencing amino acids in a protein, of the intact protein and several of the large peptide fragments.
- To analyze the smaller peptides, manual Edman degradation was performed.
- To get fragmentation of the peptide chain, enzymatic digestion was performed using trypsin, chymotrypsin, and thermolysin. These are enzymes used to break down protein.
- To find the final overlap, the researchers digested the polypeptide with a staphylococcal protease specific for glutamoyl bonds, i.e., an enzyme that cuts proteins at glutamoyl bonds.
Findings and Conclusion
- By undertaking these procedures, the researchers were able to show homology between phospholipase A2 from horse pancreas and snake venom phospholipases A2.
- The horse pancreas enzyme is also closely related to the enzyme from porcine (pig) pancreas, with the caveat that some revision should be applied to the previously published amino acid sequence of the porcine phospholipase A2 for accurate comparison.
- The discovery of this homology may have implications for the study of these enzymes and their functions, as well as their potential uses in medicine or biotechnology.
Cite This Article
APA
Evenberg A, Meyer H, Gaastra W, Verheij HM, De Haas GH.
(1977).
Amino acid sequence of phospholipase A2 from horse pancreas.
J Biol Chem, 252(4), 1189-1196.
Publication
Researcher Affiliations
MeSH Terms
- Amino Acid Sequence
- Amino Acids / analysis
- Animals
- Horses
- Molecular Weight
- Oxidation-Reduction
- Pancreas / enzymology
- Peptide Fragments / analysis
- Peptide Hydrolases
- Phospholipases
Citations
This article has been cited 11 times.- Ye H, Hill J, Kauffman J, Gryniewicz C, Han X. Detection of protein modifications and counterfeit protein pharmaceuticals using isotope tags for relative and absolute quantification and matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry: studies of insulins. Anal Biochem 2008 Aug 15;379(2):182-91.
- Iijima N, Fujikawa Y, Tateishi Y, Takashima Y, Uchiyama S, Esaka M. Cloning and expression of group IB phospholipase A2 isoforms in the red sea bream, Pagrus major. Lipids 2001 May;36(5):499-506.
- Nevalainen TJ, Haapanen TJ. Distribution of pancreatic (group I) and synovial-type (group II) phospholipases A2 in human tissues. Inflammation 1993 Aug;17(4):453-64.
- Alagón AC, Molinar RR, Possani LD, Fletcher PL Jr, Cronan JE Jr, Julia JZ. Venom from the snake Bothrops asper Garman. Purification and characterization of three phospholipases A2. Biochem J 1980 Mar 1;185(3):695-704.
- Batra SP, Nicholson BH. 9-azidoacridine, a new photoaffinity label for nucleotide- and aromatic-binding sites in proteins. Biochem J 1982 Oct 1;207(1):101-8.
- Nishida S, Kim HS, Tamiya N. Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata. Biochem J 1982 Dec 1;207(3):589-94.
- Freemont PS, Dunbar B, Fothergill-Gilmore LA. The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase. Biochem J 1988 Feb 1;249(3):779-88.
- Rose K, Savoy LA, Simona MG, Offord RE, Wingfield P. C-terminal peptide identification by fast atom bombardment mass spectrometry. Biochem J 1988 Feb 15;250(1):253-9.
- Nicholson BH, Batra SP. Structural interpretation of the binding of 9-azidoacridine to D-amino acid oxidase. Biochem J 1988 Nov 1;255(3):907-12.
- Vanfleteren JR, Evers EA, Van de Werken G, Van Beeumen JJ. The primary structure of cytochrome c from the nematode Caenorhabditis elegans. Biochem J 1990 Nov 1;271(3):613-20.
- Possani LD, Alagòn AC, Fletcher PL Jr, Varela MJ, Juliá JZ. Purification and characterization of a phospholipase A2 from the venom of the coral snake, Micrurus fulvius microgalbineus (Brown and Smith). Biochem J 1979 Jun 1;179(3):603-6.
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