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  The amino-acid sequence of porcine adenylate kinase from skeletal muscle

Heil, A., Müller, G., Noda, L., Pinder, T., Schirmer, R. H., Schirmer, I., et al. (1974). The amino-acid sequence of porcine adenylate kinase from skeletal muscle. European Journal of Biochemistry, 43(1), 131-144. doi:10.1111/j.1432-1033.1974.tb03393.x.

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Heil, Albert1, Author           
Müller, Gudrun1, Author           
Noda, Lafayette, Author
Pinder, Thomas, Author
Schirmer, R. Heiner1, Author           
Schirmer, Ilse1, Author           
von Zabern, Inge1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: 1Adenylate kinase (ATP:AMP phosphotransferase) has been purified 490-fold from porcine muscle with a final yield of 60 mg/kg muscle. 2The amino-acid composition is Asp11, Asn2, Thr14, Ser11, Glu19, Gln6, Pro6, Gly19, Ala8, Cys2, Val17, Met6, Ile9, Leu18. Tyr7, Phe5, Lys21, His2, Arg11. 3The protein molecule is a single polypeptide chain of 194 amino-acid residues with an acetyl-methionine at the N-terminus and a lysine residue at the C-terminus. 4Cyanogen bromide cleavage of carboxymethylated adenylate kinase yielded six fragments which were further degraded by using trypsin, chymotrypsin, thermolysin, subtilisin or α-protease. Sequence data on the resulting peptides are summarized in the present report, full details are given in a supplementary paper which has been deposited at CNRS from where copies can be obtained. 5The primary structure of porcine adenylate kinase is: Ac-Met-Glu-Glu-Lys-Leu-Lys-Lys-Ser-Lys-Ile10-Ile-Phe-Val-Val-Gly-Gly-Pro-Gly - Ser-Gly20-Lys-Gly-Thr-Gln-Cys-Glu-Lys-Ile-Val-Gln30-Lys-Tyr-Gly-Tyr-Thr-His-Leu-Ser-Thr-Gly40-Asp-Leu-Leu-Arg-Ala-Glu-Val-Ser-Ser-Gly50-Ser-Ala-Arg-Gly-Lys-Met-Leu-Ser-Glu-Ile60-Met-Glu-Lys-Gly-Gln-Leu-Val-Pro-Leu-Glu70-Thr-Val-Leu-Asp-Met-Leu-Arg-Asp-Ala-Met80-Val-Ala-Lys-Val-Asp-Thr-Ser-Lys-Gly-Phe90-Leu-Ile-Asp-Gly-Tyr-Pro-Arg-Glu-Val-Lys100-Gln-Gly-Glu-Glu-Phe-Glu-Arg-Lys-Ile-Gly110-Gln-Pro-Thr-Leu-Leu-Leu-Tyr-Val-Asp120-Ala-Gly-Pro-Glu-Thr-Met-Thr-Lys-Arg-Leu-Leu130-Lys-Arg-Gly-Glu-Thr-Ser-Gly-Arg-Val-Asp140-Asp-Asn-Glu-Glu-Thr-Ile-Lys-Lys-Arg-Leu150-Glu-Thr-Tyr-Tyr-Lys-Ala-Thr-Glu-Pro-Val160-Ile-Ala-Phe-Tyr-Glu-Lys-Arg-Gly-Ile-Val170-Arg-Lys-Val-Asn-Ala-Glu-Gly-Ser-Val-Asp180-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu190-Asp-Thr-Leu-Lys.

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Language(s): eng - English
 Dates: 1973-08-291973-11-232005-03-031974-03
 Publication Status: Issued
 Pages: 14
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 Rev. Type: Peer
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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 43 (1) Sequence Number: - Start / End Page: 131 - 144 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040