Studies on the composition of pig serum lipoproteins. Isolation and characterization of different apoproteins.
Biochim Biophys Acta
; 393(1): 88-99, 1975 May 30.
Article
en En
| MEDLINE
| ID: mdl-166686
1. Different lipoprotein density fractions from pig serum were isolated by phosphotungstate precipitation followed by purification in the preparative ultra-centrifuge. 2. The protein part of very low density lipoproteins was composed of approximately 52 percent lipoprotein B apoprotein and the rest of lipoprotein C II apoprotein and other as yet unidentified peptides. 3. The protein moiety of low density lipoproteins consisted primarily of lipoprotein B apoprotein (over 95 percent); the amino acid compositions of lipoprotein B apoprotein of very low and low density lipoproteins were practically identical. 4. The predominant polypeptide of pig serum high density lipoproteins exhibited an amino acid composition and a molecular weight very similar to human liprotein A I apoprotein. In contrast to human lipoprotein A I apoprotein, the apoprotein from pigs was found to release leucine first followed by alanine, threonine, and lysine upon incubation with carboxypeptidase A. 5. In pig serum the major lipoprotein C apoprotein was found to be a polypeptide similar in amino acid composition to lipoprotein C II apoprotein from human serum. The molecular weight of this polypeptide is approximately 8000. Incubation experiments with carboxypeptidase A indicate serine to be the most likely C-terminal amino acid.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Apoproteínas
/
Lipoproteínas
Límite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1975
Tipo del documento:
Article
Pais de publicación:
Países Bajos