Protein synthesis in vitro by pig blastocyst tissue before attachment

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Abstract
The nature of protein synthesis in the elongated blastocyst before definitive attachment was compared with that in the uterine endometrium from the same animal. The effect of estradiol-17.beta. on the incorporation of leucine into blastocyst tissue proteins was also studied. [3H]Leucine was incorporated into soluble protein by the pregnant sow blastocyst (trophoblast) tissue. Gel electrophoresis revealed a major component labeled in the .beta.-glycoprotein region. There was negligible activity in the section of the gel corresponding to albumin, or pre- or post-albumin. In the presence of estradiol-17.beta. the profile of [3H]leucine incorporation into proteins was similar to that of the control sample, though incorporation was slightly reduced when 100 .mu.g estradiol was included in the medium. The pattern of [3H]leucine incorporation into soluble proteins by endometrial tissue from the same animal differed from that of trophoblast tissue. Endometrium from a 3rd animal at the same stage of pregnancy was used to show that the pattern of incorporation was similar whether the tissue was blended or minced before incubation. There was a very low [3H]leucine incorporation into soluble proteins with a mobility similar to that of the 2 major soluble protein components recovered from trophoblast incubations, but a high incorporation in that part of the gel ranging from the post-albumin to the pre-albumin region. Under these experimental conditions there was no detectable effect of estrogens on the quantitative or qualitative pattern of protein synthesis.

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