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Parathyroid Hormone in Human Plasma: IMMUNOCHEMICAL CHARACTERIZATION AND BIOLOGICAL IMPLICATIONS
G V Segre1, J F Habener, D Powell
1Endocrine Unit, Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts 02114.
Most circulating parathyroid hormone (PTH) in humans lacks the amino-terminal region, suggesting it is biologically inactive. This finding helps explain variations in PTH measurements and its immunoreactivity in plasma.
Area of Science:
- Endocrinology
- Immunochemistry
- Biochemistry
Background:
- Parathyroid hormone (PTH) is crucial for calcium and phosphate homeostasis.
- Understanding PTH structure and immunoreactivity is vital for diagnosing endocrine disorders.
- Previous studies have shown heterogeneity in circulating PTH levels.
Purpose of the Study:
- To characterize the antigenic recognition of anti-bovine parathyroid hormone antisera.
- To investigate the immunochemical similarities between bovine and human parathyroid hormone.
- To determine the structure of immunoreactive parathyroid hormone in human plasma.
Main Methods:
- Antisera reactivity was tested against various bovine PTH fragments and human PTH.
- Antisera were modified by preincubation with hormone fragments to restrict recognition.
- Radioimmunoassay and gel filtration were used to analyze PTH in human plasma.
Main Results:
- All antisera recognized multiple antigenic determinants on PTH.
- Modified antisera revealed greater similarity between bovine and human PTH in the amino-terminal region.
- Circulating human PTH predominantly lacks the amino-terminal portion, including the 14-19 region.
Conclusions:
- The dominant form of immunoreactive PTH in human plasma is a fragment lacking amino-terminal reactivity.
- This structural characteristic contributes to the heterogeneity observed in plasma PTH measurements.
- The majority of immunoreactive PTH in human circulation is likely biologically inactive due to this deletion.
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