INTERFERON SEQUENCE HOMOLOGY AND RECEPTOR BINDING ACTIVITY OF OVINE TROPHOBLAST ANTILUTEOLYTIC PROTEIN
- 1 November 1987
- journal article
- research article
- Published by Bioscientifica in Journal of Endocrinology
- Vol. 115 (2) , R13-R15
- https://doi.org/10.1677/joe.0.115r013
Abstract
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 α-interferon; 28% of the remaining amino acid changes were conservative. 125I-Labelled human α-interferon bound to membrane receptors from sheep uteri with an approximate Kd of 4 × 10−11 M; binding was inhibited by unlabelled α-interferon or purified blastocyst antiluteolytic protein. The blastocyst antiluteolytic protein therefore closely resembles the interferon-α family of antiviral proteins.This publication has 12 references indexed in Scilit:
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