Biol. Bull. Sign up for etocs!
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shimomura, O.
Right arrow Articles by Flood, P. R.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Shimomura, O.
Right arrow Articles by Flood, P. R.

The Biological Bulletin, Vol 194, Issue 3 244-252, Copyright © 1998 by Marine Biological Laboratory

CELL BIOLOGY

Luciferase of the Scyphozoan Medusa Periphylla periphylla

O. Shimomura and P. R. Flood
Marine Biological Laboratory, Woods Hole, Massachusetts 02543; Department of Physiology, Boston University School of Medicine, Boston, Massachusetts 02118

Two types of luciferase that catalyze the luminescent oxidation of coelenterazine were isolated from the marginal exumbrella epithelium (lappet) and the ovary of Periphylla periphylla; they were designated luciferase-L and luciferase-O, respectively. Luciferase-L (Mr 32,000), probably derived from highly specialized photocytes, was very resistant to heat, and its activity was little affected by boiling; but it was unstable in solutions of low ionic strength if bovine serum albumin was not included in the solvent. Luciferase-O (Mr 75,000) occurred in the eggs in association with particulate matter, and was solubilized and extracted with a buffer containing 2 M guanidine hydrochloride; the enzyme was highly stable in this strongly denaturing solvent. The intensities of the coelenterazine luminescence catalyzed by both luciferases were maximal at pH 7.8 and in the presence of about 1 M NaCl. The quantum yield of coelenterazine was estimated to be 0.14 with luciferase-L (emission max. at 465 nm) and 0.12 with luciferase-O (emission max. at 470 nm). The luminescence caused by both luciferases was strongly inhibited by Cu2+ and thiol compounds.


This article has been cited by other articles:


Home page
 Biol. Bull.Home page
O. Shimomura, P. R. Flood, S. Inouye, B. Bryan, and A. Shimomura
Isolation and Properties of the Luciferase Stored in the Ovary of the Scyphozoan Medusa Periphylla periphylla
Biol. Bull., December 1, 2001; 201(3): 339 - 347.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by the Marine Biological Laboratory.