An aprotinin binding site localized in the hormone binding domain of the estrogen receptor from calf uterus.
It has been proposed that the estrogen receptor bears proteolytic activity responsible for its own transformation. This activity was inhibited by aprotinin. Incubation of transformed ER with aprotinin modified the proteolytic digestion of the hormone binding subunit by proteinase K. The smallest hormone-binding fragment of the ER, obtained by tryptic digestion, was still able to bind to aprotinin. These results suggest that aprotinin interacts with ER and the hormone-binding domain of ER is endowed with a specific aprotinin-binding site.
Istituto di Patologia Generale ed Oncologia, III Cattedra I Facoltà di Medicina e Chirurgia, Napoli, Italy.
V
V
Nigro
N
N
Medici
C
C
Abbondanza
S
S
Minucci
B
B
Moncharmont
A M
AM
Molinari
G A
GA
Puca
D000818:Animals; D007611:Aprotinin / Q000378:metabolism*; D001665:Binding Sites; D002417:Cattle; D019286:Endopeptidase K; D005260:Female; D011960:Receptors, Estrogen / Q000187:drug effects / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000494:pharmacology; D014357:Trypsin / Q000494:pharmacology; D014599:Uterus / Q000187:drug effects / Q000378:metabolism*
D011960:Receptors, Estrogen; D007611:Aprotinin; D012697:Serine Endopeptidases; D014357:Trypsin; D019286:Endopeptidase K