Indicate the presence of numerical data in the abstract (whether numerical data plays a key role in medical records), solely using the information from the abstract.
--------
Question: Abstract: The apolipoprotein B-100 (apoB-100) gene in leukocytes and the apoB-100 messenger RNA (mRNA) and translated apolipoprotein in the livers from normal and abetalipoproteinemic individuals were evaluated. Four complementary DNA probes for apoB-100 covering the 5', middle, and 3' regions of the apoB-100 mRNA were utilized and Southern blot analysis indicated that the apoB-100 gene is present in abetalipoproteinemia without major insertions or deletions. Polyadenylated hepatic apoB-100 mRNA from two abetalipoproteinemic patients was normal in size, and the concentration of apoB-100 mRNA was increased sixfold compared with control hepatic apoB-100 mRNA levels. ApoB-100 was detected in hepatocytes of abetalipoproteinemic patients by immunohistochemical techniques. These results indicate that the biochemical defect in abetalipoproteinemic patients studied is most consistent with a posttranslational defect in apoB-100 processing or secretion with an up-regulation of the apoB-100 mRNA.
Question: Does the abstract contain any numerical data?

Answer: Yes

Question: Abstract: A 52K glycoprotein is secreted by human breast cancer cells in culture after estrogen stimulation. Using monoclonal antibodies, we have quantitated and characterized the corresponding proteins of the cell compartment. Using pulse-chase experiments, we have shown that about 40% of the 52K protein is secreted, the majority being successively processed into a 48K and a 34K protein. This last protein is very stable. The processing is inhibited by lysosomotropic agents and leupeptin, suggesting that it occurs in acidic vesicles, such as lysosomes or endosomes. Estradiol increased the intracellular level of immunoreactive 52K related proteins by 4-fold. Its effect is, however, more obvious in the medium, since there is a constitutive level in the cell. The stimulatory effects of estradiol on [3H]mannose and [35S]methionine incorporation into these proteins were similar and the endoglycosydase H sensitivity of the proteins was not altered, suggesting that estradiol did not modulate the glycosylation step. Antiestrogens did not stimulate synthesis and glycosylation of the 52K related proteins. Estradiol also increased the stability of the 52K precursor as well as that of total proteins. We conclude that the secreted 52K protein is the precursor of two cellular proteins of 48K and 34K. Estradiol stimulates both the intracellular accumulation of these proteins and the secretion of the precursor.
Question: Does the abstract contain any numerical data?

Answer: Yes

Question: Abstract: The effects of at least three doses of each of five orally administered progestins on estrogen-primed, postmenopausal endometrial biochemistry and morphologic features were analyzed. The progestins tested were norethindrone, medroxyprogesterone acetate (MPA), norgestrel, dydrogesterone, and progesterone. The dose required to elicit responses similar to those seen in premenopausal, secretory endometria was assessed for each of the parameters measured, and the relative potencies were calculated. Potencies, relative to a value of 1 for norethindrone, are L norgestrel 8 (D/L norgestrel 4), MPA 0.1, dydrogesterone 0.02, and progesterone 0.002. The dose of norethindrone required to elicit secretory phase activity was about 0.35 mg/day. These values agree with published data obtained with the use of different methods (delay of menstruation in premenopausal women, endometrial histologic features of estrogen-primed, ovariectomized women).
Question: Does the abstract contain any numerical data?

Answer:
Yes