Covalent structure of apolipoprotein A-II from Macaca mulatta serum high-density lipoproteins. [Apolipoprotein]
The covalent structure of apolipoprotein A-II, isolated from the serum high-density lipoprotein of a single male Rhesus monkey (Macaca mulatta), was determined. The amino acid sequence of this 77-residue polypeptide is: < Glu-Ala-Glu-Glu-Pro/sup 5/-Ser-Val-Glu-Ser-Leu/sup 10/-Val-Ser-Gln-Tyr-Phe/sup 15/-Gln-Thr-Val-Thr-Asp/sup 20/-Tyr-Gly-Lys-Asp-Leu/sup 25/-Met-G lu-Lys-Val-Lys/sup 30/-Ser-Pro-Glu-Leu-Gln/sup 35/-Ala-Gln-Ala-Lys-Ala/sup 40/-Tyr-Phe-Glu-Lys-Ser/sup 45/-Lys-Glu-Gln-Leu-Thr/sup 50/-Pro-Leu-Val-Lys-Lys/sup 55/-Ala-Gly-Thr-Asp-Leu/sup 60/-Val-Asn-Phe-Leu-Ser/sup 65/-Tyr-Phe-Val-Glu-Leu/sup 70/-Arg-Thr-Gln-Pro-Ala/sup 75/-Thr-Gln-COOH. A comparison of this structure to that of the monomeric form of human apolipoprotein A-II reveals a high degree of homology except for six conservative amino acid replacements (positions 3, 6, 40, 53, 59, and 71). Of particular structural significance is the replacement of cysteine by serine in position 6. This explains why Rhesus A-II exists in monomeric form, contrary to the established dimeric nature of the human protein.
- Research Organization:
- Univ. of Chicago
- OSTI ID:
- 7187547
- Journal Information:
- Biochemistry; (United States), Vol. 15:6
- Country of Publication:
- United States
- Language:
- English
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