Green flavoprotein fromP. leiognathi: Purification, characterization and identification as the product of thelux G(N) gene
✍ Scribed by Raibekas, Andrei A.
- Publisher
- John Wiley and Sons
- Year
- 1991
- Weight
- 593 KB
- Volume
- 6
- Category
- Article
- ISSN
- 0884-3996
No coin nor oath required. For personal study only.
✦ Synopsis
A green flavoprotein (GFP) was isolated and purified t o homogeneity from
Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54000 and contains t w o molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.