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Sequence of horse (Equus caballus) apoA-II. Another example of a dimer forming apolipoprotein.
Abstract: Apolipoprotein A-II, the second major apolipoprotein of human HDL, also has been observed in a variety of mammals; however, it is either present in trace amounts or absent in other mammals. In humans and chimpanzee, and probably in other great apes, apoA-II with a cysteine at residue 6 is able to form a homodimer. In other primates as well as other mammals, apoA-II, lacking a cysteine residue, is monomeric. However, horse HDL has been reported to contain dimeric apoA-II that following reduction forms monomers. In this report, we extend these observations by reporting on the first complete sequence for a horse apolipoprotein and by demonstrating that horse apoA-II also contains a cysteine residue at position 6. Both the intact protein and its enzymatic fragments were analyzed by chemical sequence analysis and time-of-flight MALDI-MS (matrix assisted laser desorption ionization mass spectrometry). We also obtained molecular mass data on dimeric and monomeric apoA-II using electrospray-ionization mass spectrometry (ESI-MS). The data are compared with other mammalian sequences of apoA-II and are discussed in terms of resulting similarities and variations in the primary sequences.
Publication Date: 2004-07-16 PubMed ID: 15253869DOI: 10.1016/j.cbpc.2004.02.008Google 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.
- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- Non-P.H.S.
- Research Support
- U.S. Gov't
- P.H.S.
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.
This research article focuses on an in-depth analysis and sequencing of a type of protein found in horses, named as ‘apoA-II’. Previously only discovered in human HDL, in this study, the researchers found out that horses also contain this protein, particularly having a cysteine (amino acid) at the same position as in humans and chimpanzees.
Introduction to Apolipoprotein A-II
- The research focuses on Apolipoprotein A-II (apoA-II), which is the second major protein related to human HDL (High-Density Lipoprotein).
- This protein has been identified in various mammals typically in trace amounts or not at all.
- In species like humans and chimpanzees, and possibly in other great apes, apoA-II can form a homodimer, which is a complex of two identical molecules, due to a cysteine (an essential amino acid) at its 6th residue.
Horse Apolipoprotein A-II
- The paper presents an interesting discovery that Horse HDL (High-Density Lipoprotein) also contains apoA-II, and it has the ability to form a homodimer.
- It is observed that after reduction, this dimeric apoA-II in horses forms monomers (single unique molecules).
- The researchers have expanded these discoveries by analyzing the first complete sequence of a horse apolipoprotein.
Analysis and Results
- The intact protein along with its broken fragments were studied via chemical sequence analysis and a time-of-flight MALDI-MS (Matrix Assisted Laser Desorption Ionization Mass Spectrometry) technique.
- They also gathered molecular mass data for dimeric and monomeric apoA-II using ESI-MS (Electrospray Ionization Mass Spectrometry).
- This allowed them to demonstrate that horse apoA-II contains a cysteine residue in the 6th position, similar to humans and other primates.
Comparison and Discussion
- Data obtained from the analysis are compared with other mammalian sequences of apoA-II.
- The researches also discussed the variations and similarities in the primary sequences observed.
Cite This Article
APA
Puppione DL, Fischer WH, Park M, Whitelegge JP, Schumaker VN, Golfeiz S, MacDonald MH.
(2004).
Sequence of horse (Equus caballus) apoA-II. Another example of a dimer forming apolipoprotein.
Comp Biochem Physiol B Biochem Mol Biol, 138(3), 213-220.
https://doi.org/10.1016/j.cbpc.2004.02.008 Publication
Researcher Affiliations
- Boyer Hall, The Molecular Biology Institute and The Department of Chemistry and Biochemistry, University of California at Los Angeles, Los Angeles, CA 90095, USA. puppione@chem.ucla.edu
MeSH Terms
- Amino Acid Sequence
- Animals
- Apolipoprotein A-II / metabolism
- Dimerization
- Horses
- Humans
- Molecular Sequence Data
- Sequence Homology, Amino Acid
- Spectrometry, Mass, Electrospray Ionization
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Citations
This article has been cited 1 times.- Puppione DL, Della Donna L, Laganowsky AD, Bassilian S, Souda P, Ryder OA, Whitelegge JP. Mass spectral analyses of the two major apolipoproteins of great ape high density lipoproteins. Comp Biochem Physiol Part D Genomics Proteomics 2009 Dec;4(4):305-309.
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