Interferon sequence homology and receptor binding activity of ovine trophoblast antiluteolytic protein.
Sequencing of the 40 N-terminal amino acids of the blastocyst protein responsible for blocking corpus luteum regression in early pregnancy in sheep revealed a 37% homology with human alpha-interferon; 28% of the remaining amino acid changes were conservative. 125I-Labelled human alpha-interferon bound to membrane receptors from sheep uteri with an approximate Kd of 4 x 10(-11) M; binding was inhibited by unlabelled alpha-interferon or purified blastocyst antiluteolytic protein. The blastocyst antiluteolytic protein therefore closely resembles the interferon-alpha family of antiviral proteins.
Stewart
H J
HJ
AFRC Institute of Animal Physiology and Genetics Research, Babraham, Cambridge.
McCann
S H
SH
Barker
P J
PJ
Lee
K E
KE
Lamming
G E
GE
Flint
A P
AP
D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D007370:Interferon Type I / Q000378:metabolism*; D008186:Luteolytic Agents / Q000037:antagonists & inhibitors; D008969:Molecular Sequence Data; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012756:Sheep
D007370:Interferon Type I; D008186:Luteolytic Agents; D011257:Pregnancy Proteins; D011956:Receptors, Cell Surface; C020947:interferon tau