Etmopterus lantern sharks use coelenterazine as the substrate for their luciferin-luciferase bioluminescence system

نویسندگان

چکیده

The lantern shark genus Etmopterus contains approximately 40 species of deep-sea bioluminescent cartilaginous fishes. They emit blue light mainly from the ventral body surface. biological functions this bioluminescence have been discussed based on luminescence patterns, but mechanism remains uncertain. In study, we detected both coelenterazine and coelenterazine-dependent luciferase activity in photophore tissue molleri. results suggested that sharks is produced using as substrate for luciferin-luciferase reaction, some luminous bony

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Length at ¢rst maturity of two species of lantern sharks (Etmopterus spinax and Etmopterus pusillus) o¡ southern Portugal

Etmopterus spinax and Etmopterus pusillus are captured in large quantities in some deep-water ¢sheries along the Portuguese coast and are always discarded. Specimens were collected from February 2003 to May 2004 from deep-water ¢sheries and classi¢ed as mature or immature. Maturity ogives were ¢tted and size at ¢rst maturity estimated for each sex of each species. Both species are late maturing...

متن کامل

Can coelenterates make coelenterazine? Dietary requirement for luciferin in cnidarian bioluminescence.

In the calcium-activated photoprotein aequorin, light is produced by the oxidation of coelenterazine, the luciferin used by at least seven marine phyla. However, despite extensive research on photoproteins, there has been no evidence to indicate the origin of coelenterazine within the phylum Cnidaria. Here we report that the hydromedusa Aequorea victoria is unable to produce its own coelenteraz...

متن کامل

Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase.

The Renilla bioluminescent system in vivo is comprised of three proteins--the luciferase, green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called luciferin-binding protein (LBP). This work reports the cloning of the full-size cDNA encoding CBP from soft coral Renilla muelleri, its overexpression and properties of the recombinant protein. The apo-CBP was quantitati...

متن کامل

Studies on the Oxidation of Luciferin without Luciferase and the Mechanism of Bioluminescence

In five groups of luminous animals it can be shown that luminescence is connected with the oxidation of a substance, luciferin, in aqueous solution, in presence of an enzyme, luciferase, and dissolved oxygen. In the mollusc, Pholas dactylus, Dubois (1) has been able to oxidize Pholas luciferin with luminescence by KMn04, HzO, BaOz, PbOa, and hypochlorites. I have been unable to oxidize with lum...

متن کامل

Firefly luciferase can use L-luciferin to produce light.

L-Luciferin is a competitive inhibitor of firefly luciferase with a K1 between 3 and 4 microM. Furthermore L-luciferin can serve as an alternative substrate for light production. Catalysis of L-luciferin can be observed in the absence of, or at low concentrations of, D-luciferin. The light production from L-luciferin increases slowly (maximal half-time 8 min) to a stable plateau. At low concent...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Biochemical and Biophysical Research Communications

سال: 2021

ISSN: ['0006-291X', '1090-2104']

DOI: https://doi.org/10.1016/j.bbrc.2021.09.007