Ovine prolactin and human growth hormone derivatives. Specific modification of their alpha-amino groups.
The alpha-amino group of ovine prolactin (oPRL) and human growth hormone (hGH) was selectively modified by transamination with glyoxylic acid. No difference was found in the binding capacity of transaminated oPRL to rat liver lactogenic receptors with respect to its control, although both samples showed a decrease in its binding capacity with reference to the native hormone. This decrease was due to conformational changes caused by the reaction conditions and not by the transamination itself, as shown by the circular dichroism spectra. Transaminated hGH retained the full binding capacity of the hormone. These results suggest that the alpha-amino group is not relevant for the binding to lactogenic liver receptors in both lactogenic hormones.
Caridad
J J
JJ
Institute of Biochemistry and Biophysics, (UBA-CONICET), Faculty of Pharmacy and Biochemistry, Buenos Aires, Argentina.
Nowicki
C
C
Santomé
J A
JA
Wolfenstein-Todel
C
C
D000818:Animals; D001667:Binding, Competitive; D002942:Circular Dichroism; D013006:Growth Hormone / Q000031:analogs & derivatives* / Q000138:chemical synthesis*; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D011388:Prolactin / Q000031:analogs & derivatives* / Q000138:chemical synthesis* / Q000378:metabolism; D011487:Protein Conformation; D011981:Receptors, Prolactin / Q000378:metabolism; D012756:Sheep; D013329:Structure-Activity Relationship
D011981:Receptors, Prolactin; D011388:Prolactin; D013006:Growth Hormone