TY - JOUR
T1 - An aprotinin binding site localized in the hormone binding domain of the estrogen receptor from calf uterus
AU - Nigro, Vincenzo
AU - Medici, Nicola
AU - Abbondanza, Ciro
AU - Minucci, Saverio
AU - Moncharmont, Bruno
AU - Molinari, Anna Maria
AU - Puca, Giovanni Alfredo
PY - 1990/7/31
Y1 - 1990/7/31
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(90)92180-8
DO - 10.1016/0006-291X(90)92180-8
M3 - Article
C2 - 1696480
AN - SCOPUS:0024988242
VL - 170
SP - 930
EP - 936
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -