Characterization and amino-terminal sequence of apolipoprotein AI from plasma high density lipoproteins in the preruminant calf, bos Spp
| Autor: | Laurence Beaubatie, Doris A. Sparrow, Sylvie Auboiron, James T. Sparrow, Dominique Bauchart, P. Michel Laplaud, M. John Chapman |
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| Rok vydání: | 1990 |
| Předmět: |
Alanine
Apolipoprotein A-I Molecular Sequence Data Age Factors Biophysics Cell Biology Glutamic acid Biology Biochemistry Molecular biology Glutamine Valine Aspartic acid Animals Cattle lipids (amino acids peptides and proteins) Amino Acid Sequence Isoleucine Leucine Lipoproteins HDL Molecular Biology Peptide sequence Apolipoproteins A |
| Zdroj: | Biochemical and Biophysical Research Communications. 166:833-839 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(90)90885-q |
| Popis: | The major apolipoprotein of calf plasma high-density lipoproteins, apo-AI, has been isolated and characterized. Apolipoprotein AI (apo-AI) was separated from the protein moiety of high-density lipoproteins (d 1.090-1.180 g/ml) by preparative electrophoresis in SDS-polyacrylamide gels followed by electrophoretic elution. Purified calf apo-AI had an Mr of approx. 27,000-28,000 in SDS-polyacrylamide gels, resembling human apo-AI. The amino acid composition of calf apo-AI displayed an overall similarity to that of its human and other mammalian counterparts (baboon, dog, badger, rabbit, rat and mouse), but differed in having higher proportions of glutamic acid, alanine and isoleucine. Amino-terminal amino acid sequence analysis up to the 47th residue showed close homology between calf apo-AI and those of the mammals with which it was compared. However, residues 2, 7, 20 and 22 in calf AI (i.e. aspartic acid, serine, glutamic acid and isoleucine, respectively) were substituted by glutamic acid, proline or glutamine, aspartic acid, and valine or leucine respectively, in the other mammals. |
| Databáze: | OpenAIRE |
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