Serum α1-acid glycoprotein (α1-ag) in bovine fetuses and newborn calves was characterized. Serum α1-ag concentration increased during fetal development and neonatal stages. Mean ± sd serum α1-ag concentration reached a peak of 1,368 ± 207 μg/ml immediately after birth, but thereafter gradually decreased to 249 ± 100 μg/ml, similar to the normal adult bovine range.
By use of isoelectric focusing of thin-layer gels, we detected 7 microheterogeneity bands ranging from pI 3.2 to 3.8 in adult bovine serum. Twelve bands ranging from pI 2.6 to 3.8 were found in 9-month fetuses and in neonates. The 5 most-acidic bands, which are absent in adult serum, ranged between pI 2.6 and 3.1 and decreased with maturation as band patterns assumed adult characteristics.
By crossed affinity electrophoresis, α1-ag of adult bovine serum was separated into 4 peaks according to its differential affinity to concanavalin A (conA). Seventy-five percent of the α1-ag concentration was represented by peak 3 (P-3) and peak 4 (P-4), which had moderate or strong binding to conA. In contrast, fetal sera contained only peak 1 (P-1), which did not have conA-binding affinity. In neonatal sera, 4 peaks were recognized, of which P-1 comprised 70% of the total α1-ag. Thereafter, with aging, percentage of P-3 and P-4 increased as band composition approached the normally expected adult pattern.
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