+ Translate

The primary structure of chicken muscle acylphosphatase isozyme Ch2

, : The primary structure of chicken muscle acylphosphatase isozyme Ch2. Journal of Biochemistry 102(5): 1221-1229

The amino acid sequence of one, Ch2, of the two isozymes of chicken muscle acylphosphatase was determined. It consists of 98 amino acid residues with N-acetylalanine at the amino(N)-terminus and contains no cysteine: Ac-Ala-Gly-Ser-Glu-Gly-Leu-Met-Ser-Val-Asp-Tyr-Glu-Val-Ser-Gly-Arg-Val-Gln-Gly-Val-Phe-Phe-Arg-Lys-Tyr-Thr-Gln-Ser-Glu-Ala-Lys-Arg-Leu-Gly-Leu-Val-Gly-Trp-Val-Arg-Asn-Thr-Ser-His-Gly-Thr-Val-Gln-Gly-Gln-Ala-Gln-Gly-Pro-Ala-Ala-Arg-Val-Arg-Glu-Leu-Gln-Glu-Trp-Leu-Arg-Lys-Ile-Gly-Ser-Pro-Gln-Ser-Arg-Ile-Ser-Arg-Ala-Glu-Phe-Thr-Asn-Glu-Lys-Glu-Ile-Ala-Ala-Leu-Glu-His-Thr-Asp-Phe-Gln-Ile-Arg-Lys-COOH. The sequence differs in 44% of the total positions from the other isozyme, Ch1. Comparison of the sequence and the predicted conformational profile of Ch2 with those of Ch1 suggests that they share a common evolutionary origin and appear to have retained similar conformations throughout their evolutionary origin and appear to have retained similar conformation throughout their evolutionary development.

(PDF 0-2 workdays service)

Accession: 006740879

PMID: 2830254

Submit PDF Full Text: Here

Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:

Related references

Minowa, O.; Ohba, Y.; Mizuno, Y.; Shiokawa, H., 1987: The primary structure of chicken muscle acylphosphatase isozyme Ch1. 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-...

Camici, G.; Manao, G.; Cappugi, G.; Berti, A.; Stefani, M.; Liguri, G.; Ramponi, G., 1983: The primary structure of turkey muscle acylphosphatase. The complete primary structure of turkey muscle acylphosphatase has been determined. The sequence was derived from peptides obtained by digestion of the carboxymethylated protein with pepsin and thermolysin and by subdigestion of some of the cyano...

Manao, G.; Camici, G.; Modesti, A.; Liguri, G.; Berti, A.; Stefani, M.; Cappugi, G.; Ramponi, G., 1984: Human skeletal muscle acylphosphatase: the primary structure. Human skeletal muscle acylphosphatase, purified by a technique based on affinity chromatography on immunoadsorbent, has been sequenced completely using tryptic and peptic peptide series, prepared by reverse-phase high-pressure liquid chromatograph...

Pechere, J.F., 1967: Purification of muscle acylphosphatase of chicken breast. Bulletin de la Societe de Chimie Biologique 49(7): 897-899

Ohba, Y.; Mizuno, Y.; Takasawa, T.; Shiokawa, H., 1985: Two isozymes of chicken muscle acylphosphatase: purification and properties. Two acylphosphatases, named Ch1 and Ch2, have been purified from chicken skeletal muscle. The molecular weights were determined to be 11,900 and 12,000 for Ch1 and Ch2, respectively, by sedimentation equilibrium. In the amino acid compositions of...

Ohba, Y.; Mizuno, Y.; Shiokawa, H., 1989: Ontogenic expression of the two isozymes, Ch1 and Ch2, of chicken muscle acylphosphatase. Activities of the two isozymes, Ch1 and Ch2, of chicken muscle acylphosphatase were measured in breast muscles, leg muscles, and livers of developing chicks from day 11 in ovo to day 15 of free life. Measurement was performed using rabbit antibodi...

Tashian R.E.; Stroup S.K.; Y.Y.S.L.; Henriksson D., 1978: Primary structure of an isozyme of carbonic anhydrase isolated from bovine skeletal muscle. Federation Proceedings 37(6): 1797

Saudek V.; Williams R.J.P.; Ramponi G., 1988: Secondary structure of acylphosphatase from rabbit skeletal muscle a nmr study. Journal of Molecular Biology 199(1): 233-237

Taddei, N.; Magherini, F.; Chiti, F.; Bucciantini, M.; Raugei, G.; Stefani, M.; Ramponi, G., 1996: C-terminal region contributes to muscle acylphosphatase three-dimensional structure stabilisation. Ser-Ala and Ser-Ala-Ser-Ala C-terminus elongated (DELTA+2 and DELTA+4, respectively) and two C-terminus deleted (DELTA-2 and DELTA-3) muscle acylphosphatase mutants were investigated to assess the catalytic and structural roles of the C-terminal r...

Saudek V.; Wormald M.R.; Williams R.J.P.; Boyd J.; Stefani M.; Ramponi G., 1989: Identification and description of beta structure in horse muscle acylphosphatase by nmr spectroscopy. Nuclear magnetic resonance spectra of acylphosphatase were searched for signs of .beta.-structure, i.e. characteristic nuclear Overhauser enhancement patterns displayed in the two-dimensional spectra, typical chemical shifts, coupling constants an...