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Extraction and purification of calcium-activated photoproteins from the ctenophores Mnemiopsis sp. and Beroe ovata

Journal Article · · Biochemistry; (United States)
OSTI ID:6543452
Calcium-activated bioluminescent ''photoproteins'' from the ctenophores Mnemiopsis sp. and Beroue ovata have been isolated by extraction with EDTA and purified 3800-fold and 7800-fold, respectively. The steps consisted of ammonium sulfate and protoamine sulfate treatments, followed by several steps of ion-exchange, gel filtration, and solubility chromatography. The purified photoproteins are virtually homogeneous by the criterion of sodium dodecyl sulfate polyacrylamide gel electrophoresis. Approximately 30,000 adult specimens of Mnemiopsis, totalling more than 600 kg wet wt, yielded 2 mg of purified photoprotein. Mnemiopsis photoprotein has been resolved into two functionally identical forms (''isoproteins''), termed mnemiopsin-1 and mnemiopsin-2, by chromatography on DEAE-cellulose. Berovin, the Beroue photoprotein, chromatographs as a single symmetrical peak under the same conditions.
Research Organization:
Johns Hopkins Univ., Baltimore
OSTI ID:
6543452
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 13:7; ISSN BICHA
Country of Publication:
United States
Language:
English