期刊论文详细信息
FEBS Letters
Complete amino acid sequence of the sarcoplasmic calcium‐binding protein (SCP‐I) from crayfish (Astacus leptodactilus)
Cox, J.A.2  Jauregui-Adell, J.1  Wnuk, W.2 
[1] Centre de Recherches de Biochimie Macromoléculaire du Centre National de la Recherche Scientifique, Boîte Postale 5051, F-34033 Montpellier Cedex, France;Département de Biochimie, Université de Genève, Quai Ernest-Ansermet 30, CH-1211 Genève 4, Switzerland
关键词: Chain;    α-;    Sarcoplasmic protein;    Ca2+-binding protein;    Amino acid sequence;    (Astacus leptodactylus);    PV;    parvalbumin;    SCP;    sarcoplasmic calcium-binding protein;    CaBP;    calcium-binding protein;   
DOI  :  10.1016/0014-5793(89)80131-0
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

The complete amino acid sequence of the alpha chain of the dimeric sarcoplasmic Ca2+-binding protein (SCP-I=α2) from crayfish (Astacus leptodactylus) has been determined by partial automatic sequencing of the peptides derived from tryptic digests of the protein after citraconylation or treatment with 1,2-cyclohexanedione. Overlapping peptides were obtained by cleavage with o-iodosobenzoic acid, or digestion with Staphylococcus aureus protease, thermolysin and pepsin. The acetylated N-terminus was identified by fast atom bombardment mass spectrometry. The monomeric protein contains 192 amino acids and has an M r of 21 643. The sequence shows the presence of three calcium-binding sites and perhaps of two others that may be degenerated.

【 授权许可】

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