Multiple Immunoreactive Molecular Forms of Parathyroid Hormone in Human Serum

1972 ◽  
Vol 140 (4) ◽  
pp. 1393-1398 ◽  
Author(s):  
J. M. Canterbury ◽  
E. Reiss
Keyword(s):  
Parathyroid Hormone ◽  
Human Serum ◽  
Molecular Forms

A radioimmunoassay for human parathyroid hormone utilizing a goat anti-bovine PTH serum

1981 ◽  
Vol 96 (2) ◽  
pp. 215-221 ◽  
Author(s):  
L. E. Mallette
Keyword(s):  
Parathyroid Hormone ◽  
Primary Hyperparathyroidism ◽  
Secondary Hyperparathyroidism ◽  
Human Serum ◽  
Central Region ◽  
Antigenic Site ◽  
Human Parathyroid Hormone ◽  
Domestic Goat ◽  
Standard Serum ◽  
Dilution Curves

Abstract. An antiserum (NG-1) against bovine PTH (bPTH) generated in the domestic goat was characterized for use in the radioimmunoassay of PTH in human serum. When a carboxyterminal fragment of bPTH is used as radioligand, this antiserum detects only an antigenic site in the central region of the hPTH molecule. The synthetic hormone fragment, hPTH-(44-68), will displace 93% of the tracer, after which the addition of intact hPTH causes no further displacement. The assay does not detect the synthetic aminoterminal 1-34 fragment of the bovine or human hormones, nor the carboxyterminal fragment of the human hormone, hPTh-(53-84). Standard curves with bPTH-(1-84) and partially purified hPTH are not parallel, so that hPTH is used as standard. Serum from subjects with uraemia or primary hyperparathyroidism gives dilution curves parallel to that with the hPTH standard. The assay with NG-1 has been applied to the diagnosis of primary and secondary hyperparathyroidism, used to monitor the disappearance of PTH after parathyroidectomy, and for measurement of PTH in selective venous samples.

Parathyroid hormone-related protein in human term placenta and membranes

1994 ◽  
Vol 142 (2) ◽  
pp. 217-224 ◽  
Author(s):  
S J Bowden ◽  
J F Emly ◽  
S V Hughes ◽  
G Powell ◽  
A Ahmed ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Caesarean Section ◽  
Amniotic Fluid ◽  
Elective Caesarean Section ◽  
Molecular Forms ◽  
Molecular Heterogeneity ◽  
Related Protein ◽  
Human Term Placenta ◽  
Parathyroid Hormone Related Protein ◽  
Spontaneous Labour

Abstract Parathyroid hormone-related protein (PTHrP), the hypercalcaemia of malignacy factor, is expressed in the tissues of the human uteroplacental unit, including the placenta, amnion and chorion. We have used three region-specific immunoassays to quantitate and compare the distribution of PTHrP in tissues obtained at term following spontaneous labour and vaginal delivery or elective Caesarean section. In non-labouring women highest PTHrP(1–86) and (37–67) immunoreactivity was found in amnion covering the placenta, rather than the decidua parietalis of the uterus (reflected amnion) (median 1020 vs 451 fmol/g; 2181 vs 1444 fmol/g respectively). In labouring women, the PTHrP(1–86) concentration in reflected amnion was inversely correlated with the interval between rupture of the membranes and delivery. Tissue PTHrP(1–86) concentrations were lower in placenta than in chorion and amnion (medians 12, 109 and 664 fmol/g respectively) and, in all tissues, PTHrP(1–34) and (37–67) concentrations were significantly higher than that of PTHrP(1–86). Bioactive PTHrP(1–34) was detected in placenta, chorion and amnion using the ROS cell bioassay. The PTHrP(1–86) concentration (mean ± s.e.m.=41·4 ± 4·5 pmol/l) was high in amniotic fluid at term, although in maternal and cord plasma levels were only modestly increased. The molecular forms of PTHrP present in tissues and amniotic fluid were investigated by column chromatography which confirmed its molecular heterogeneity and suggested that processing is tissue-specific and occurs at both amino- and carboxy-terminals of the peptide. Journal of Endocrinology (1994) 142, 217–224

Multiple forms of parathyroid hormone-like proteins in a human tumour

1989 ◽  
Vol 2 (1) ◽  
pp. 11-20 ◽  
Author(s):  
H. M. Docherty ◽  
D. A. Heath
Keyword(s):  
Parathyroid Hormone ◽  
Carcinoid Tumour ◽  
Molecular Forms ◽  
Osteosarcoma Cell ◽  
Multiple Forms ◽  
Human Tumour ◽  
Chromatographic Characterization ◽  
Positively Charged

ABSTRACT The extensive chromatographic characterization of four parathyroid hormone (PTH)-like proteins in a human bronchial carcinoid tumour associated with humoral hypercalcaemia and severe osteitis fibrosa is described. PTH-like bioactivity was detected in acetic acid extracts of the tumour using an in-vitro osteosarcoma cell bioassay. The active tumour proteins were positively charged at physiological pH and had apparent Mr of approximately 29 000, 16 000, 4000–9000 and < 4000. The proteins were immunologically distinct from PTH, but each stimulated PTH-sensitive adenylate cyclase in cultured osteoblastic cells. There was no evidence of PTH gene expression by the tumour. These proteins represent different molecular forms of PTH-related protein.

Form and folding of pentameric human serum Amyloid P component

2002 ◽  
Vol 217 (7-8) ◽  
Author(s):  
A. Janner
Keyword(s):  
Human Serum ◽  
Quaternary Structure ◽  
Point Group ◽  
Serum Amyloid ◽  
Molecular Forms ◽  
Golden Mean ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

AbstractThe molecular prismatic forms which enclose the tertiary and the quaternary structure of the human serum Amyloid P component show remarkable ratios expressible in terms of the golden mean. A scale-rotation crystallographic point group, leaving these forms invariant, allows to explain these golden mean proportions and to assign integer indices to the vertices of the molecular forms.

scholarly journals Distribution of iron between the binding sites of transferrin in serum: methods and results in normal human subjects

Blood ◽  
1979 ◽  
Vol 53 (6) ◽  
pp. 1058-1065 ◽  
Author(s):  
A Leibman ◽  
P Aisen
Keyword(s):  
Human Serum ◽  
Binding Sites ◽  
Human Subjects ◽  
Molecular Forms ◽  
Crossed Immunoelectrophoresis ◽  
Relative Binding ◽  
Normal Human ◽  
Diferric Transferrin ◽  
A Site ◽  
Acid Labile

When it is incompletely saturated with iron, transferrin may exist in four molecular forms: apotransferrin, monoferric (A) transferrin (with iron occupying only the A site of the protein), monoferric (B) transferrin, and diferric transferrin. By combining electrophoresis in urea-polyacrylamide gels with crossed immunoelectrophoresis using specific antihuman transferin antiserum, it is possible to display and estimate the concentration of each of these four forms in normal human serum. The distribution of iron between the binding sites of transferrin is neither random nor determined by the relative binding strengths of transferrin's two sites. Rather, the more weakly binding and acid-labile B site of the protein is predominantly occupied.

scholarly journals Heterogeneity of carboxyl-terminal parathyroid hormone circulating forms in patients with hyperparathyroidism due to end stage renal disease

2009 ◽  
Vol 53 (9) ◽  
pp. 1074-1078 ◽  
Author(s):  
José Gilberto H. Vieira ◽  
Ilda S. Kunii ◽  
Monique N. Ohe ◽  
Aluizio B. Carvalho
Keyword(s):  
Parathyroid Hormone ◽  
Renal Disease ◽  
End Stage Renal Disease ◽  
Molecular Forms ◽  
Clinical Aspects ◽  
Intact Pth ◽  
Serum Samples ◽  
Carboxyl Terminal ◽  
Stage Renal Disease ◽  
End Stage

OBJECTIVE: To study carboxyl-terminal (COOH) parathyroid hormone (PTH) circulating forms in patients with hyperparathyroidism due to end stage renal disease (ESRD). METHODS: An immunometric assay that recognizes both intact and COOH PTH forms was developed. The assay, in conjunction with an intact assay, was used to measure PTH in serum samples obtained from 25 patients with hyperparathyroidism due to ESRD. Samples were also submitted to gel filtration chromatography in a Superdex® 30 1.6 x 60 cm column, and the PTH content in the elution tubes, measured using both assays. RESULTS: Values from 39.000 to 232.300 ng/mL (mean ± sd = 101.680 ± 45.330 ng/mL) were found using the COOH assay (PTH 39-84 was used as standard). Values obtained by the intact PTH assay ranged from 318 to 3.307 ng/mL (1.769 ± 693 ng/mL) with a correlation between assays of 0.462 (p = 0.02). The elution profile obtained using the COOH assay showed a preponderance of forms with MW ranging from 8.500 to 4.500 daltons. The profiles obtained from the 25 patients were very similar. CONCLUSIONS: In patients with hyperparathyroidism due to ESRD circulating PTH levels contain a broad range of molecular forms including COOH with MW ranging from 8.500 to 4.500 daltons. These forms are not recognized by the standard intact PTH assays. The correlation of these findings to the clinical aspects of bone disease in ESRD patients remains to be studied.

Nanostructured Au-Pt hybrid disk electrodes for enhanced parathyroid hormone detection in human serum

2019 ◽  
Vol 128 ◽  
pp. 165-174 ◽  
Author(s):  
Ajay Kumar Yagati ◽  
Anna Go ◽  
Sachin Ganpat Chavan ◽  
Changyoon Baek ◽  
Min-Ho Lee ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Human Serum ◽  
Disk Electrodes

Assay of Parathyroid Hormone in Human Serum and its Uses

1976 ◽  
Vol 13 (1-6) ◽  
pp. 549-554 ◽  
Author(s):  
J. S. Woodhead ◽  
D. A. Walker
Keyword(s):  
Differential Diagnosis ◽  
Parathyroid Hormone ◽  
Human Serum ◽  
No Value ◽  
Clinical Application ◽  
Calcium Metabolism ◽  
Clinical Problem ◽  
Plasma Calcium ◽  
Biochemical Data ◽  
Health And Disease

The assay of parathyroid hormone has contributed greatly to our understanding of calcium metabolism in health and disease. The most important clinical application of the assay is in the differential diagnosis of hypercalcaemia, which is an increasing clinical problem. PTH assays are of little or no value in the absence of other biochemical data, especially accurate determinations of plasma calcium and phosphate.

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