Sequence of horse ( Equus caballus) apoA-II. Another example of a dimer forming apolipoprotein

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 fo...

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Veröffentlicht in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2004-07, Vol.138 (3), p.213-220
Hauptverfasser: Puppione, Donald L, Fischer, Wolfgang H, Park, Minkyu, Whitelegge, Julian P, Schumaker, Verne N, Golfeiz, Shoulamit, MacDonald, Melinda H
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container_end_page 220
container_issue 3
container_start_page 213
container_title Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
container_volume 138
creator Puppione, Donald L
Fischer, Wolfgang H
Park, Minkyu
Whitelegge, Julian P
Schumaker, Verne N
Golfeiz, Shoulamit
MacDonald, Melinda H
description 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.
doi_str_mv 10.1016/j.cbpc.2004.02.008
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subjects Amino Acid Sequence
Animals
Anti-microbial
Apolipoprotein A-II - metabolism
Dimerization
Heterodimer
Horses
Humans
Methionine sulfoxide
Molecular Sequence Data
Senescence
Sequence Homology, Amino Acid
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Thyroid binding proteins
title Sequence of horse ( Equus caballus) apoA-II. Another example of a dimer forming apolipoprotein
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