1. The amino acid sequence of human chorionic gonadotropin. The alpha subunit and beta subunit
F J Morgan, S Birken, R E Canfield J Biol Chem. 1975 Jul 10;250(13):5247-58.
The amino acid sequences of both the alpha and beta subunits of human chorionic gonadotropin have been determined. The amino acid sequence of the alpha subunit is: Ala - Asp - Val - Gln - Asp - Cys - Pro - Glu - Cys-10 - Thr - Leu - Gln - Asp - Pro - Phe - Ser - Gln-20 - Pro - Gly - Ala - Pro - Ile - Leu - Gln - Cys - Met - Gly-30 - Cys - Cys - Phe - Ser - Arg - Ala - Tyr - Pro - Thr - Pro-40 - Leu - Arg - Ser - Lys - Lys - Thr - Met - Leu - Val - Gln-50 - Lys - Asn - Val - Thr - Ser - Glu - Ser - Thr - Cys - Cys-60 - Val - Ala - Lys - Ser - Thr - Asn - Arg - Val - Thr - Val-70 - Met - Gly - Gly - Phe - Lys - Val - Glu - Asn - His - Thr-80 - Ala - Cys - His - Cys - Ser - Thr - Cys - Tyr - Tyr - His-90 - Lys - Ser. Oligosaccharide side chains are attached at residues 52 and 78. In the preparations studied approximately 10 and 30% of the chains lack the initial 2 and 3 NH2-terminal residues, respectively. This sequence is almost identical with that of human luteinizing hormone (Sairam, M. R., Papkoff, H., and Li, C. H. (1972) Biochem. Biophys. Res. Commun. 48, 530-537). The amino acid sequence of the beta subunit is: Ser - Lys - Glu - Pro - Leu - Arg - Pro - Arg - Cys - Arg-10 - Pro - Ile - Asn - Ala - Thr - Leu - Ala - Val - Glu - Lys-20 - Glu - Gly - Cys - Pro - Val - Cys - Ile - Thr - Val - Asn-30 - Thr - Thr - Ile - Cys - Ala - Gly - Tyr - Cys - Pro - Thr-40 - Met - Thr - Arg - Val - Leu - Gln - Gly - Val - Leu - Pro-50 - Ala - Leu - Pro - Gin - Val - Val - Cys - Asn - Tyr - Arg-60 - Asp - Val - Arg - Phe - Glu - Ser - Ile - Arg - Leu - Pro-70 - Gly - Cys - Pro - Arg - Gly - Val - Asn - Pro - Val - Val-80 - Ser - Tyr - Ala - Val - Ala - Leu - Ser - Cys - Gln - Cys-90 - Ala - Leu - Cys - Arg - Arg - Ser - Thr - Thr - Asp - Cys-100 - Gly - Gly - Pro - Lys - Asp - His - Pro - Leu - Thr - Cys-110 - Asp - Asp - Pro - Arg - Phe - Gln - Asp - Ser - Ser - Ser - Ser - Lys - Ala - Pro - Pro - Pro - Ser - Leu - Pro - Ser-130 - Pro - Ser - Arg - Leu - Pro - Gly - Pro - Ser - Asp - Thr-140 - Pro - Ile - Leu - Pro - Gln. Oligosaccharide side chains are found at residues 13, 30, 121, 127, 132, and 138. The proteolytic enzyme, thrombin, which appears to cleave a limited number of arginyl bonds, proved helpful in the determination of the beta sequence.
2. Primary structure of murine major histocompatibility complex alloantigens: amino acid sequence of the amino-terminal one hundred and seventy-three residues of the H-2Kb glycoprotein
H Uehara, B M Ewenstein, J M Martinko, S G Nathenson, J E Coligan, T J Kindt Biochemistry. 1980 Jan 22;19(2):306-15. doi: 10.1021/bi00543a009.
The amino-terminal 173 residues of the murine histocompatibility antigen H-2Kb have been assigned by using radiochemical methodology. The complete sequence of an 86 residue glycopeptide (CN-Ib), which is one of the five major CNBr fragments of Kb, was determined by analysis of peptides obtained from digests using thrombin and V8 staphylococcal protease. Complete sequences were obtained for the three large thrombic peptides, and these were aligned by using peptides from the V8 protease digest. Alignment of the CNBr fragments was carried out by using [35S]Met-labeled peptides from a tryptic digest of the papain-cleaved H-2Kb molecule. Positive identification was possible for all the common amino acids except Asp (Asp) which was indirectly assigned and which is designated in italics. The sequence obtained in our studies was Gly-Pro-His-Ser-Leu-Arg-Tyr-Phe-Val-Thr-Ala-Val-Ser-Arg-Pro-Gly-Leu-Gly-Glu-Pro-Arg-Tyr-Met-Glu-Val-Gly-Tyr-Val-Asp-Asp-Thr-Glu-Phe-Val-Arg-Phe-Asp-Ser-Asp-Ala-Glu-Asn-Pro-Arg-Tyr-Glu-Pro-Arg-Ala-Arg-Trp-Met-Glu-Gln-Glu-Gly-Pro-Glu-Tyr-Trp-Glu-Arg-Glu-Thr-Gln-Lys-Ala-Lys-Gly-Asn-Glu-Gln-Ser-Phe-Arg-Val-Asp-Leu-Arg-Thr-Leu-Leu-Gly-Tyr-Tyr-(Asn)-Gln-Ser-Lys-Gly-Gly-Ser-His-Thr-Ile-Gln-Val-Ile-Ser-Gly-Cys-Glu-Val-Gly-Ser-Asp-Gly-Arg-Leu-Leu-Arg-Gly-Tyr-Gln-Gln-Tyr-Ala-Tyr-Asp-Gly-Cys-Asp-Tyr-Ile-Ala-Leu-Asn-Glu-Asp-Leu-Lys-Thr-Trp-Thr-Ala-Ala-Asp-Met-Ala-Ala-Leu-Ile-Thr-Lys-His-Lys-Trp-Glu-Gln-Ala-Gly-Glu-Ala-Glu-Arg-Leu-Arg-Ala-Tyr-Leu-Glu-Gly-Thr-Cys-Val-Glu-Trp-Leu-Arg-Arg-Tyr-Leu-Lys. These data represent the longest reported amino acid sequence determined by utilizing radiochemical methodology and provide the first extensive information on the primary structure of murine histocompatibility antigens.
3. The primary structure of human liver manganese superoxide dismutase
D Barra, M E Schinina, M Simmaco, J V Bannister, W H Bannister, G Rotilio, F Bossa J Biol Chem. 1984 Oct 25;259(20):12595-601.
The complete amino acid sequence of manganese superoxide dismutase from human liver was determined. The sequence was deduced following characterization of the peptides obtained from tryptic, chymotryptic, and Staphylococcus aureus digests of the apoprotein. Chemical cleavage with dimethyl sulfoxide-hydrobromic acid was also carried out. The amino acid sequence listed below is made up of 196 amino acids and the two subunit polypeptides in the native enzyme appear to be identical. No homology was observed with copper/zinc containing class of superoxide dismutase. Lys-His-Ser-Leu-Pro-Asp-Leu-Pro-Tyr-Asp-Tyr-Gly-Ala-Leu-Glu-Pro-His-Il e -Asn-Ala-Gln-Ile-Met-Gln-Leu-His-His-Ser-Lys-His-His-Ala-Ala-Tyr-Val-Asn -Asn-Leu-Asn-Val-Thr-Gln-Glu-Lys-Tyr-Gln-Glu-Ala-Leu-Ala-Lys-Gly-Asp-Val -Thr-Ala-Gln-Ile-Ala-Leu-Gln-Pro-Ala-Leu-Lys-Phe-Asn-Gly-Gly-Gly-His-Ile -Asn-His-Ser-Ile-Phe-Trp-Thr-Asn-Leu-Ser-Pro-Asn-Gly-Gly-Gly-Gln-Pro-Lys -Gly-Glu-Leu-Leu-Glu-Ala-Ile-Lys-Arg-Asp-Phe-Gly-Ser-Phe-Asp-Lys-Phe-Lys -Gln-Lys-Leu-Thr-Ala-Ala-Ser-Val-Gly-Val-Gln-Gly-Ser-Gly-Trp-Leu-Gly-Phe -Asn-Lys-Gln-Arg-Gly-His-Leu-Gln-Ile-Ala-Ala-Cys-Pro-Asn-Gln-Asp-Pro-Leu -Gln-Gly-Thr-Thr-Gly-Leu-Ile-Pro-Leu-Leu-Gly-Ile-Asp-Val-Trp-Glu-His-Ala -Tyr-Tyr-Leu-Gln-Tyr-Lys-Asn-Val-Arg-Pro-Asp-Tyr-Leu-Lys-Ala-Ile-Trp-Asn -Val-Ile-Asn-Trp-Glu-Asn-Val-Thr-Glu-Arg-Tyr-Met-Ala-Cys-Lys-Lys.
