Enzymatic deglycosylation of human thyroglobulin: fluorescence studies.
Biochim Biophys Acta
; 957(1): 105-10, 1988 Nov 02.
Article
en En
| MEDLINE
| ID: mdl-3179315
The interaction between the carbohydrate and the amino acid residues in human thyroglobulin has been studied. Previous reports showed that the removal of the two terminal carbohydrates of the complex chains leads to an increase in thyroglobulin binding to thyroid membranes. In our study, after enzymatic release with glycosidases of the sugar moieties from thyroglobulin, a time-dependent decrease in tryptophan fluorescence has been observed. This decrease was also associated with a shift in the emission peak from 335 to 340 nm. The strong quenching of tryptophan emission was also accompanied by a decrease in the exposure of tryptophan residues, as shown by a Stern-Volmer analysis with the neutral quencher acrylamide. These data, together with the increase in fluorescence of the dansylated deglycosylated thyroglobulin, strongly suggest that a significant conformational change of thyroglobulin follows the deglycosylation of the protein.
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Bases de datos:
MEDLINE
Asunto principal:
Tiroglobulina
/
Glicoproteínas
Límite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1988
Tipo del documento:
Article
País de afiliación:
Italia