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.

[Q]: Abstract: With the use of initial records of 1128 women who presented for interval tubal ligation, characteristics of those who were sterilized were juxtaposed with characteristics of those who did not return for surgery. Follow-up telephone interviews were conducted to explore regret after sterilization among 268 sterilized women. The subsequent histories of 144 women who did not return for surgery were examined, to determine whether failure to return might have screened, selectively, the women at greatest risk of regret. High levels of subsequent unwanted conception and pregnancy wastage were found in the nonreturn group. Institutional factors were often implicated in failure to return. Variables available at initial presentation are proposed to identify women who risk adverse consequences of postponed sterilization, to facilitate return without increasing regret.
Question: Does the abstract contain any numerical data?
[A]: Yes

[Q]: Abstract: The ultimate cause of destruction of red blood cells (RBCs) after oxidative damage with Heinz body formation is not well understood. We correlated the changes in RBC morphology and membrane protein composition after oxidant treatment with the alterations in deformability of whole cells and cell membranes. The incubation of RBCs with phenylhydrazine concentrations of 0.3 to 100 mg/dL at 37 degrees C for one hour led to a dose-dependent formation of Heinz bodies, ranging from isolated Heinz bodies at 1 mg/dL to a confluent coating of the inner membrane surface at 100 mg/dL phenylhydrazine. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of a large quantity of hemoglobin bound to the ghost membrane of treated RBCs. Electrophoresis with and without dithiothreitol indicated that disulfide bridges are abundant between hemoglobin molecules and are also present among membrane proteins but are not the major bond between hemoglobin and membrane. Changes of spectrin, ankyrin, band 3, and band 6 and the appearance of a 260,000-dalton complex were also observed. With phenylhydrazine concentrations below 30 mg/dL, even in the presence of multiple Heinz bodies, the RBC deformability measured by filtration through 2.6-, 4.5-, and 6.8-microns pores and the membrane deformability determined by a filter aspiration technique were not altered. With 100 mg/dL phenylhydrazine, when the entire membrane was coated with Heinz bodies, RBC filterability and membrane deformability were drastically reduced. These results indicate that oxidative damage of RBCs with discrete Heinz body formation causes focal membrane rigidification but does not affect the global cellular deformability until the Heinz bodies nearly cover the entire cell endoface.
Question: Does the abstract contain any numerical data?
[A]: Yes

[Q]: Abstract: From a single cell fusion, five stable hybridomas secreting antiovine placental lactogen (oPL) antibodies were obtained. Three of these secrete immunoglobulin (Ig)G subclass, and the other two secrete IgM class antibodies. Ascites fluids were raised in mice for each clone and were used as the antibody component for the development of solid phase RIA. Three solid-phase RIAs were successfully established using individual IgG subclass monoclonal antibodies, but the IgM class antibodies were ineffective. In all three individual solid-phase RIAs, the binding of [125I]iodo-oPL to the immobilized antibody was inhibited by unlabeled oPL, but not by ovine pituitary PRL (oPRL), ovine GH (oGH), or ovine pituitary extract. Two of the IgG subclass antibodies were able to inhibit the binding of [125I] iodo-oPL to PRL receptors(s) and to GH receptor(s) in rabbit mammary gland and liver, respectively. One of these two IgG subclass antibodies was more effective at inhibiting the binding of oPL to PRL receptor(s) in rabbit mammary gland, whereas the other one is more effective in inhibiting the binding of oPL to GH receptor(s) in rabbit liver. These antibodies, however, could only weakly inhibit the binding of [125I]iodo-oPRL to rabbit mammary gland and were ineffective in inhibiting the binding of [125I]iodo-oGH to rabbit liver. The addition of monoclonal antibodies in both radioreceptor assay (RRA) for PRL (RRA-PRL) and for GH (RRA-GH) did not affect the parallelism of the displacement curve of oPL standard. Our results suggest that oPL might contain two distinct binding sequence(s): one responsible for the binding of oPL to PRL receptor(s) and the other responsible for the binding of oPL to GH receptor(s). These two binding sequences might overlap or be located adjacent to one another. The interaction of monoclonal antibodies with these binding sequences of oPL may block the binding of oPL with PRL and GH receptor(s). Alternatively, our studies suggest that the monoclonal antibodies do not bind to hormone receptor(s)-binding sequence(s) in oPL, but the interaction between oPL and monoclonal antibody might alter the conformational structure of the oPL which will consequently lead to a lower binding of oPL to PRL and GH receptor(s).
Question: Does the abstract contain any numerical data?
[A]:
Yes