Amino acid sequence of the Ca2+-triggered luciferin binding protein of Renilla reniformis
S Kumar, M Harrylock, KA Walsh, MJ Cormier… - FEBS letters, 1990 - Elsevier
The complete amino acid sequence of the Ca 2+-triggered luciferin binding protein (LBP) of
Renilla reniformis has been determined. The apoprotein has an unblocked amino terminus …
Renilla reniformis has been determined. The apoprotein has an unblocked amino terminus …
Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase
MS Titushin, SV Markova, LA Frank… - Photochemical & …, 2008 - Springer
The Renilla bioluminescent system in vivo is comprised of three proteins—the luciferase,
green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called …
green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called …
[HTML][HTML] Ca2+-induced bioluminescence in Renilla reniformis. Purification and characterization of a calcium-triggered luciferin-binding protein.
H Charbonneau, MJ Cormier - Journal of Biological Chemistry, 1979 - Elsevier
A Ca2+-triggered luciferin-binding protein (BP-LH2) from the bioluminescent marine
coelenterate, Renilla reniformis, has been purified by conventional methods. One kilogram …
coelenterate, Renilla reniformis, has been purified by conventional methods. One kilogram …
Mechanism of calcium induction of Renilla bioluminescence. Involvement of a calcium-triggered luciferin binding protein
J Anderson, H Charbonneau, M Cormier - Biochemistry, 1974 - ACS Publications
James Michael Anderson, Harry Charbonneau, and Milton J. Cormier* abstract: When
extracts of bioluminescent Anthozoans, such as Renilla, are prepared in the presence of …
extracts of bioluminescent Anthozoans, such as Renilla, are prepared in the presence of …
Expression, purification and characterization of calcium-triggered luciferin-binding protein of Renilla reniformis
S Inouye - Protein expression and purification, 2007 - Elsevier
The Ca2+-triggered luciferin-binding protein of Renilla reniformis (RLBP) is a non-covalent
complex of apoprotein (apoRLBP) and coelenterazine (luciferin). The gene encoding …
complex of apoprotein (apoRLBP) and coelenterazine (luciferin). The gene encoding …
Expression and characterization of EF-hand I loop mutants of aequorin replaced with other loop sequences of Ca 2+ -binding proteins: an approach to …
S Inouye, Y Sahara-Miura - The journal of biochemistry, 2016 - academic.oup.com
The binding properties of Ca 2+ to EF-hand I of aequorin (AQ) were characterized by
replacing the loop sequence of EF-hand I (AQ [I]) with other known loop sequences of Ca 2+ …
replacing the loop sequence of EF-hand I (AQ [I]) with other known loop sequences of Ca 2+ …
Amino acid sequence of the calcium-dependent photoprotein aequorin
H Charbonneau, KA Walsh, RO McCann… - Biochemistry, 1985 - ACS Publications
The Ca (II)-dependent photoprotein aequorin produces the luminescence of the marine
coelenterate Aequorea victoria. The complete amino acid sequence of aequorin has been …
coelenterate Aequorea victoria. The complete amino acid sequence of aequorin has been …
Extraction of Renilla-type luciferin from the calcium-activated photoproteins aequorin, mnemiopsin, and berovin.
WW Ward, MJ Cormier - Proceedings of the National …, 1975 - National Acad Sciences
Photoproteins, which emit light in an oxygen-independent intramolecular reaction initiated
by calcium ions, have been isolated from several bioluminescent organisms, including the …
by calcium ions, have been isolated from several bioluminescent organisms, including the …
Cloning and sequence analysis of cDNA for the luminescent protein aequorin.
S Inouye, M Noguchi, Y Sakaki… - Proceedings of the …, 1985 - National Acad Sciences
The luminescent jellyfish Aequorea contains a photoprotein, aequorin, which emits light by
an intramolecular reaction in the presence of a trace amount of Ca2+. A cDNA library of …
an intramolecular reaction in the presence of a trace amount of Ca2+. A cDNA library of …
Cloning and sequence analysis of cDNA for the Ca2+-activated photoprotein, clytin
S Inouye, FI Tsuji - FEBS letters, 1993 - Elsevier
Clytin is a member of the aequorin family of photoproteins. It is made up of 189 amino acid
residues, contains 3 Ca 2+-binding sites, and shows 62% homology in amino acid residues …
residues, contains 3 Ca 2+-binding sites, and shows 62% homology in amino acid residues …