Plasma lipid transport in the preruminant calf,Bos spp: Primary structure of bovine apolipoprotein A-I |
| |
| Affiliation: | 1. Department of Medicine, Baylor College of Medicine and the Methodist Hospital, Houston, TX U.S.A.;2. Unité 321 INSERM, Pavilion Benjamin Delessert, Hôpital de la Pitié, Paris France;3. Unité de Recherches Métabolisme Energétique et Lipidique, INRA, Centre Clermont-Theix, St. Genès-Champanelle France;1. National Local Joint Engineering Research Center of Biodiagnostics and Biotherapy, The Second Affiliated Hospital of Medical College, Xi''an Jiaotong University, Xi''an, China;2. College of Medicine and Forensic Science, Xi''an Jiaotong University, Xi''an, China;3. Department of Pathology and Laboratory Medicine, Metabolic Diseases Institute, University of Cincinnati, Cincinnati, USA;1. Department of Neurosurgery, University of Health Sciences, Şişli Hamidiye Etfal Training and Research Hospital, İstanbul, Turkey;2. Department of Neurosurgery, Medical Faculty of Ataturk University, Erzurum, Turkey;3. Department of Pathology, Medical Faculty of Ataturk University, Erzurum, Turkey;4. Department of Child Neurology, Derince Education Research Hospital, Kocaeli, Turkey;5. Department of Neurosurgery, Medical Faculty, Recep Tayyip Erdogan University, Rize, Turkey;1. Sykehuspartner Health Enterprise, Oslo, Norway;2. Frisch Centre, Oslo, Norway;3. Department of Health Management and Health Economics, Institute of Health and Society, University of Oslo, Oslo, Norway |
| |
| Abstract: | The preruminant calf (Bos spp.) is a model of considerable interest with regard to hepatic and intestinal lipoprotein metabolism (Bauchart et al., J. Lipid Res. (1989) 30, 1499–1514 and Laplaud et al., J. Lipid Res. (1990) 31, 1781–1792). As a preliminary step towards future experiments dealing with HDL metabolism in the calf, we have purified apoA-I from this animal and determined its complete amino acid sequence. Thus, approx. 10% of calf apoA-I was shown to contain a propeptide, with the sequence Arg-His-Phe-Trp-Gln-Gln. Enzymatic cleavage of apoA-I resulted in 10 proteolytic peptides. The complete apoA-I sequence was obtained after alignment of peptides on the basis of their homologies with those from rabbit apoA-I. Thus calf apoA-I consists of 241 amino acid residues, and exhibits high sequence homology with all mammalian apoA-I's studied to date. The bovine protein contained 10 hydrophobic amphipathic helical regions, occurring between residues 43–64, 65–86, 87–97, 98–119, 120–141, 142–163, 164–184, 185–206, 207–217 and 218–241. A computer-constructed phylogenetic tree showed that bovine apoA-I was more closely related to its dog counterpart, including the presence of a single methionine, than to the corresponding macaque and human proteins. Comparative predictions of the respective antigenic structures of human and bovine apoA-I's using the Hopp-Woods algorithm indicated similar positions for all 13 detectable antigenic sites, among which 7 were of identical, or closely related, amino acid composition. This finding was confirmed by demonstration of partial immunological identity between the two proteins upon immunodiffusion analysis, a result obtained using a monospecific rabbit antiserum against bovine apoA-I. Finally, comparison of sequence homology between bovine apoA-I and the lecithin : cholesterol acyl transferase (LCAT) activating region of human apoC-I suggests that several LCAT activating domains may be present in calf apoA-I. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
