Accession Number : ADA268597


Title :   Modified Aequorin Shows Increased Bioluminescence Activity


Descriptive Note : Final progress rept. 15 Mar 90-31 Jul 92,


Corporate Author : WOODS HOLE OCEANOGRAPHIC INSTITUTION MA DEPT OF BIOLOGY


Personal Author(s) : Prasher, Douglas C


Full Text : https://apps.dtic.mil/dtic/tr/fulltext/u2/a268597.pdf


Report Date : 18 Aug 1993


Pagination or Media Count : 10


Abstract : Aequorin belongs to a unique class of photoproteins that emit light upon the binding of certain metals, calcium being the principal intracellular activator. This 'reporting function' of the metal-binding is instantaneous and is very easy to quantitate experimentally. The project objective was to develop a variety of recombinant forms of aequorin so they can be employed as metal biosensors. Three calcium-binding sites of aequorin were modified to examine their roles in the calcium-dependent luminescence as well as potentially binding other metal ions. Aequorins having Site 2 substitutions unexpectedly produce more light than wild-type aequorin.... Calcium, Bioluminescence, Photoprotein, Mutagenesis


Descriptors :   *METALS , *METAL COMPOUNDS , *BIOLUMINESCENCE , IONS , CALCIUM , PEPTIDES , PROTEINS , SITES , ION EXCHANGE , LIGHT , X RAYS , DEOXYRIBONUCLEIC ACIDS , GENES , LUMINESCENCE


Subject Categories : Biochemistry
      Organic Chemistry


Distribution Statement : APPROVED FOR PUBLIC RELEASE