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.

Abstract: Quantitative evaluation of stainable bone aluminum and measurement of bone aluminum content were done in 55 patients on chronic maintenance dialysis. All patients underwent bone biopsies. Histomorphometry of static and dynamic parameters of bone structure, bone formation and resorption, and quantitation of stainable bone aluminum at the osteoid-bone interface were performed. In addition, bone aluminum content was measured by atomic absorption spectrophotometry. Bone aluminum content was elevated in all patients (81 +/- 9.6 vs. 18 +/- 6 micrograms/g dry wt) and stainable aluminum was found in 47% of them. All patients with predominant low-turnover osteomalacia or adynamic bone disease displayed stainable bone aluminum. In contrast, stainable bone aluminum was not present in individuals with predominant-hyperparathyroid bone disease. Patients with stainable aluminum had lower bone mass (P less than 0.05), higher volume and surface of lamellar osteoid (P less than 0.01), less volume and surface of woven osteoid (P less than 0.05 and P less than 0.01), lower osteoblastic and osteoclastic indices (P less than 0.01), less doubly labelled osteoid seams, lower mineral apposition rate and lower bone formation rates (P less than 0.05 to P less than 0.01). Stainable aluminum correlated with volume of lamellar osteoid and cellular parameters of bone formation and resorption, mineral apposition rate, and bone formation rates (P less than 0.05 to P less than 0.001). In contrast, bone aluminum content correlated with volume of lamellar osteoid only (P less than 0.001). These findings indicate that stainable aluminum at the mineralization front and not aluminum content of bone reflects the histopathologic changes found in bone of dialyzed patients. 
Question: Does the abstract contain any numerical data?
Yes

Abstract: We have determined the structures of high mannose (Man) oligosaccharide units of the alpha- and beta-subunits of mouse TSH heterodimers and of free alpha-subunits. Mouse thyrotropic tumor tissue, or pituitaries from euthyroid or hypothyroid mice, were incubated with D-[2-3H]Man, homogenized, and incubated in the presence or absence of pH 3 buffer to dissociate heterodimers. Highly enriched TSH beta-subunits, or TSH heterodimers, were obtained using anti-TSH beta serum and free alpha-subunits were subsequently obtained using anti-LH alpha-serum. High Man units released by endoglycosidase H were analyzed by paper chromatography. At 1 and 3 h oligosaccharides with 8 or 9 Man residues predominated in all subunits. In all three tissue types, units with 9 Man tended to accumulate in TSH beta-subunits, whereas Man-trimming from Man9GlcNAc to Man8GlcNAc proceeded more rapidly in TSH alpha-subunits, and in free alpha-subunits. The rate of TSH beta-subunit processing was also a function of tissue type; the rate in euthyroid pituitary tissue equaled that in tumor tissue and was greater than that in hypothyroid pituitary tissue, suggesting that processing may be physiologically regulated. Hypothyroid calf serum slowed TSH alpha-subunit processing in euthyroid pituitaries. Thus, the previously reported slower processing of Man9GlcNAc to Man8GlcNAc in heterodimers as compared to free alpha-subunits is in large part due to accumulation of Man9GlcNAc in TSH beta-subunits. 
Question: Does the abstract contain any numerical data?
Yes

Abstract: Neutrophils have been shown to express a receptor for C3dg that is distinct from CR2 and is termed complement receptor type 4 (CR4). In the present study, other peripheral blood cell types were examined by indirect immunofluorescence and flow cytometry for the presence of C3dg binding activity. Specific uptake of C3dg occurred with neutrophils, platelets, and B lymphocytes, but not with eosinophils or T lymphocytes. Monocytes, contained within a mixed cell population of peripheral blood mononuclear cells and platelets, also bound C3dg, whereas purified monocytes did not. Binding of 125I-labeled glutaraldehyde-cross-linked C3dg to platelets was saturable, with an average of 1940 C3dg molecules bound per platelet at saturation (n = 8), ranging in number from 660 to 3930 molecules bound. Activation of platelets with thrombin did not consistently cause an increase in the expression of CR4 sites. 125I-C3dg binding to platelets was competitively inhibited equally well by unlabeled C3dg and iC3b, and approximately fourfold less well by C3b. The addition of platelets to elutriated monocytes generated C3dg binding activity on these cells by the formation of platelet-monocyte complexes. Thus, the CR4 on platelets accounted for the C3dg binding activity initially observed with partially purified monocytes. The adherent property of platelets may enable them to confer on certain other cell types the ability to localize C3dg-coated immune complexes or particles. 
Question: Does the abstract contain any numerical data?

Yes

