1.
Biotechnology Techniques
; 11(9): 697-700, 1997.
Artigo
em Inglês
| SES-SP, SESSP-IBPROD, SES-SP, SESSP-IBACERVO
| ID: biblio-1060896
RESUMO
The advantages of the intrinsic fluorescence of the tryptophan and the absorbance of the methionine residues of the 18 kDa-hsp - a recombinant protein from Mycobacterium leprae - was exploited here to develop a sensitive and low costs method for protein assaying. They presented linearity between 3 and 1000 ìg of protein. The correlations between intrinsic fluorescence or absorbance at 230 nm and protein contents were both superiors to 0.99. These methods can be extended to others proteins with low aromatic residue contents