1. Amino acid sequence of human tumor derived angiogenin
B L Vallee, J L Bethune, R R Lobb, J F Riordan, J W Fett, E M Alderman, D J Strydom Biochemistry . 1985 Sep 24;24(20):5486-94. doi: 10.1021/bi00341a031.
The amino acid sequence and disulfide bond pairing of human tumor derived angiogenin, the first tumor angiogenesis factor to be isolated in pure form from human sources, have been determined by conventional sequencing techniques adapted and applied to nanomole and subnanomole levels of material. Angiogenin, obtained from conditioned media of a human colonic adenocarcinoma cell line, is a single-chain protein consisting of 123 amino acids with the following sequences: less than Glu1-Asp-Asn-Ser-Arg-Tyr-Thr-His- Phe-Leu-Thr-Gln-His-Tyr-Asp15-Ala-Lys-Pro-Gln-Gly-Arg-Asp-Asp- Arg-Tyr-Cys-Glu-Ser-Ile-Met30- Arg-Arg-Arg-Gly-Leu-Thr-Ser-Pro-Cys-Lys-Asp-Ile-Asn-Thr- Phe45-Ile-His-Gly-Asn-Lys-Arg-Ser -Ile-Lys-Ala-Ile-Cys-Glu-Asn-Lys60-Asn-Gly-Asn-Pro-His-Arg-Glu-Asn -Leu-Arg-Ile -Ser-Lys-Ser-Ser75 -Phe-Gln-Val-Thr-Thr-Cys-Lys-Leu-His-Gly-Gly-Ser-Pro-Trp-Pro90-Pro -Cys-Gln-Tyr -Arg-Ala-Thr-Ala -Gly-Phe-Arg-Asn-Val-Val-Val105-Ala-Cys-Glu-Asn-Gly-Leu-Pro-Val- His-Leu-Asp-Gln-Ser-Ile-Phe120-Arg-Arg-Pro123-OH. Three disulfide bonds link the half-cystinyl residues 26-81, 39-92, and 57-107. The sequence is homologous to that of the pancreatic ribonucleases with 35% identity and many of the remaining residues conservatively replaced. Similarities are especially apparent around the major active-site residues His-12, Lys-41, and His-119 of ribonuclease which are conserved as are three of the four disulfide bonds.(ABSTRACT TRUNCATED AT 250 WORDS)
2. Amino acid sequence of bovine brain derived class 1 heparin-binding growth factor
D J Strydom, R R Lobb, J W Harper Biochemistry . 1986 Mar 11;25(5):945-51. doi: 10.1021/bi00353a001.
The major class 1 heparin-binding growth factor from bovine brain is a single-chain polypeptide of 140 amino acids with a molecular weight of 15 877. It has the amino acid sequence Phe1-Asn-Leu-Pro-Leu-Gly-Asn-Tyr-Lys-Lys-Pro-Lys-Leu-Leu- Tyr15-Cys-Ser- Asn-Gly-Gly-Tyr-Phe-Leu-Arg-Ile-Leu-Pro-Asp-Gly-Thr30-Val-Asp-Gly- Thr-Lys-Asp-Arg- Ser-Asp-Gln-His-Ile-Gln-Leu-Gln45-Leu-Cys-Ala-Glu-Ser-Ile-Gly- Glu-Val-Tyr-Ile- Lys-Ser-Thr-Glu60-Thr-Gly-Gln-Phe-Leu-Ala-Met-Asp-Thr-Asp-Gly- Leu-Leu-Tyr-Gly75- Ser-Gln-Thr-Pro-Asn-Glu-Glu-Cys-Leu-Phe-Leu-Glu-Arg-Leu- Glu90-Glu-Asn-His-Tyr- Asn-Thr-Tyr-Ile-Ser-Lys-Lys-His-Ala-Glu-Lys105-His-Trp-Phe-Val -Gly-Leu-Lys-Lys- Asn-Gly-Arg-Ser-Lys-Leu-Gly120-Pro-Arg-Thr-His-Phe-Gly-Gln-Lys -Ala-Ile-Leu-Phe-Leu-Pro-Leu135-Pro-Val-Ser-Ser-Asp140-OH. The mitogen is homologous to the class 2 heparin-binding growth factor pituitary fibroblast growth factor with about 50% of the amino acids being identical between the two mitogens.
3. The primary structure of chicken muscle acylphosphatase isozyme Ch1
Y Mizuno, H Shiokawa, O Minowa, Y Ohba J Biochem . 1987 Nov;102(5):1213-20. doi: 10.1093/oxfordjournals.jbchem.a122160.
The amino acid sequence of chicken muscle acylphosphatase isozyme Ch1 was determined. The protein consists of 102 amino acid residues, does not contain histidine, and the NH2-terminus is acetylated: Ac-Ser-Ala-Leu-Thr-Lys-Ala-Ser-Gly-Ser- Leu-Lys-Ser-Val-Asp-Tyr-Glu-Val-Phe-Gly-Arg-Val-Gln-Gly-Val-Cys-Phe-Arg- Met- Tyr-Thr-Glu-Glu-Glu-Ala-Arg-Lys-Leu-Gly-Val-Val-Gly-Trp-Val-Lys-Asn- Thr- Ser-Gln-Gly-Thr-Val-Thr-Gly-Gln-Val-Gln-Gly-Pro-Glu-Asp-Lys-Val-Asn-Ala- Met- Lys-Ser-Trp-Leu-Ser-Lys-Val-Gly-Ser-Pro-Ser-Ser-Arg-Ile-Asp-Arg-Thr-Lys- Phe-Ser- Asn-Glu-Lys-Glu-Ile-Ser-Lys-Leu-Asp-Phe-Ser-Gly-Phe-Ser-Thr-Arg-Tyr-OH. This sequence differs in 44% of the total positions from the other isozyme (Ch2) of chicken muscle acylphosphatase (Ohba et al., the accompanying paper). The sequence of Ch1 has three substitutions from that of turkey muscle acylphosphatase; these are Ser from Ala at position 9, Ser from Arg at 47, and Lys from Asn at 83. The sequence has about 80% homology with those mammalian muscle acylphosphatases.
