Complete amino acid sequence of the sarcoplasmic calcium-binding protein (SCP-I) from crayfish (Astacus leptodactylus).
The complete amino acid sequence of the alpha chain of the dimeric sarcoplasmic Ca2+-binding protein (SCP-I = alpha 2) 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 Mr of 21,643. The sequence shows the presence of three calcium-binding sites and perhaps of two others that may be degenerated.
Jauregui-Adell
J
J
Centre de Recherches de Biochimie Macromoléculaire du Centre National de la Recherche Scientifique, Montpellier, France.
Wnuk
W
W
Cox
J A
JA
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003400:Astacoidea; D002135:Calcium-Binding Proteins / Q000302:isolation & purification; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments; D012519:Sarcoplasmic Reticulum / Q000032:analysis; D014357:Trypsin
D000596:Amino Acids; D002135:Calcium-Binding Proteins; D010446:Peptide Fragments; D014357:Trypsin