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Determination of the amino acid sequence of an intramolecular disulfide linkage‐containing sperm‐activating peptide by tandem mass spectrometry
Author(s) -
Yoshino Ken-ichi,
Takao Toshifumi,
Shimonishi Yasutsugu,
Suzuki Norio
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80663-n
Subject(s) - fast atom bombardment , peptide , chemistry , tandem mass spectrometry , mass spectrometry , peptide sequence , disulfide linkage , sea urchin , protein mass spectrometry , residue (chemistry) , cystine , intramolecular force , amino acid , cyclic peptide , chromatography , tandem mass tag , isobaric labeling , biochemistry , stereochemistry , cysteine , proteomics , biology , enzyme , paleontology , gene , quantitative proteomics
A sperm‐activating peptide (SAP) was isolated from the egg jelly of the sea urchin Stomopneustes variolaris . The presence of an intramolecular disulfide linkage in the peptide was demonstrated by fast atom bombardment (FAB) mass spectrometry with the intact and reduced peptides. The amino acid sequence of the reduced peptide was determined to be Lys‐Phe‐Cys‐Pro‐Glu‐Gly‐Lys‐Cys‐Val by tandem mass spectrometry from the spectrum produced by a collision‐induced decomposition method. Furthermore, it was also demonstrated that SAPs obtained from sea urchins Arbacia punctulata and Glyptpcidaris crenularis are cyclic peptides containing one cystine residue by FAB mass spectrometry.