Mass spectrometric evidence for a disulfide bond in aequorin regeneration.
Tryptic digests of purified recombinant apoaequorin were analyzed, before and after reduction with DTT, by fast atom bombardment mass spectrometry. The results showed that apoaequorin contains a disulfide bond between Cys145 and Cys152 and that the reduction of this bond is involved in the regeneration of aequorin.
Ohmiya
Y
Y
PRESTO, JRDC, Solar Energy Research Group, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
Kurono
S
S
Ohashi
M
M
Fagan
T F
TF
Tsuji
F I
FI
D000331:Aequorin / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D004220:Disulfides / Q000032:analysis*; D004229:Dithiothreitol / Q000494:pharmacology; D004926:Escherichia coli / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D037401:Scyphozoa; D016339:Spectrometry, Mass, Fast Atom Bombardment / Q000379:methods; D014357:Trypsin
D004220:Disulfides; D010446:Peptide Fragments; D011994:Recombinant Proteins; D000331:Aequorin; D014357:Trypsin; D004229:Dithiothreitol