Conjugation of a fetuin glycopeptide to human follicle-stimulating hormone and its subunits by photoactivation.
Human follicle-stimulating hormone (human FSH), dansylated human FSH, human FSH-alpha and human FSH-beta subunits were individually conjugated by photoactivation to an azidobenzoyl derivative of a glycopeptide isolated from fetuin. The conjugates were purified on a column of Sephadex G-100. The carbohydrate content of the conjugated human FSH increased 2.7-fold with a concomitant 1.5- and 2-fold increase in the immunological and biological activity of the human FSH. The glucosamine content of the human FSH-alpha and human FSH-beta increased 6- and 1.4-fold, respectively, after conjugation. Human FSH-alpha conjugate, when recombined with untreated human FSH-beta showed up to 50% increase in the biological activity over the control. When the conjugated human FSH-beta was combined with untreated human FSH-alpha, there was little change in the biological activity. These experiments demonstrate that the photoactivation procedure, although random and site-nonspecific in nature, provides a potential means of attachment of glycopeptides to the protein moiety and enhancement of the hormonal activity of human FSH.
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D005640:Follicle Stimulating Hormone; D006801:Humans; D046911:Macromolecular Substances; D010777:Photochemistry; D011485:Protein Binding; D000509:alpha-Fetoproteins
D046911:Macromolecular Substances; D000509:alpha-Fetoproteins; D005640:Follicle Stimulating Hormone