IMMUNOLOGICAL PROPERTIES OF SYNTHETIC HUMAN PARATHYROID HORMONE 53–84 FRAGMENT

1979 ◽  
Vol 80 (1) ◽  
pp. 153-155 ◽  
Author(s):  
G. N. HENDY ◽  
R. M. MANNING ◽  
M. ROSENBLATT ◽  
G. W. TREGEAR ◽  
H. T. KEUTMANN ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Synthetic Peptide ◽  
Terminal Region ◽  
Human Parathyroid Hormone ◽  
Enzymic Digestion ◽  
Immunological Properties ◽  
Carboxyl Terminal

The immunological properties of a synthetic peptide comprising the carboxyl-terminal 53–84 region of human parathyroid hormone (PTH) have been studied. The immunoreactivity of the synthetic human PTH-(53–84) peptide paralleled that of a 53–84 fragment of the native human hormone prepared by enzymic digestion, in both a standard radioimmunoassay, which was not region-specific, and also a radioimmunoassay specific for the carboxyl-terminal region of PTH. However, in both types of radioimmunoassay the synthetic human PTH-(53–84) peptide was four to five times more reactive than the native human PTH-(53–84) fragment.

Human Parathyroid Hormone: Immunological Properties of the Amino Terminus and of Synthetic Fragments

1974 ◽  
Vol 47 (6) ◽  
pp. 567-576 ◽  
Author(s):  
G. N. Hendy ◽  
P. M. Barling ◽  
J. L. H. O'Riordan
Keyword(s):  
Parathyroid Hormone ◽  
Synthetic Peptides ◽  
Terminal Region ◽  
Amino Terminus ◽  
Human Parathyroid Hormone ◽  
Immunological Properties ◽  
Immunological Assay ◽  
Amino Terminal

1. Immunological assay systems specific to the amino-terminal region of parathyroid hormone were used to study the properties of human parathyroid hormone (HPTH 1-84) and of synthetic peptides. One of these peptides (HPTH 1-34A) had the sequence proposed by Niall, Sauer, Jacobs, Keutmann, Segre, O'Riordan, Aurbach & Potts (1974). The others (HPTH 1-34B and C, synthesized by different methods) had the sequence proposed by Brewer, Fairwell, Ronan, Sizemore & Arnaud (1972). 2. HPTH 1-84 and HPTH 1-34A behaved identically in a number of these systems. In some systems, especially those using antisera obtained by immunizing with HPTH 1-34A, differences were, however, found. These may be due to conformational or other physical differences or to the presence of an immunologically incomplete site in the fragment. 3. In systems in which HPTH 1–84 and HPTH 1-34A behaved identically the peptides with the sequence proposed by Brewer et al. (1972) were of low reactivity by 100–2000-fold.

Human Parathyroid Hormone: Synthesis and Chemical, Biological, and Immunological Evaluation of the Carboxyl-Terminal Region*

Endocrinology ◽  
1978 ◽  
Vol 103 (3) ◽  
pp. 978-984 ◽  
Author(s):  
MICHAEL ROSENBLATT ◽  
GINO V. SEGRE ◽  
GEOFFREY W. TREGEAR ◽  
GARY L. SHEPARD ◽  
GEORGE A. TYLER ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Terminal Region ◽  
Human Parathyroid Hormone ◽  
Hormone Synthesis ◽  
Carboxyl Terminal ◽  
Immunological Evaluation

scholarly journals Short carboxyl terminal parathyroid hormone peptides modulate human parathyroid hormone signaling in mouse osteoblasts

2021 ◽  
Vol 572 ◽  
pp. 15-19
Author(s):  
Kittrawee Kritmetapak ◽  
Ravinder J. Singh ◽  
Theodore A. Craig ◽  
Jolaine M. Hines ◽  
Rajiv Kumar
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Signaling ◽  
Human Parathyroid Hormone ◽  
Carboxyl Terminal

scholarly journals Receptors Specific for the Carboxyl-Terminal Region of Parathyroid Hormone on Bone-Derived Cells: Determinants of Ligand Binding and Bioactivity

Endocrinology ◽  
2005 ◽  
Vol 146 (4) ◽  
pp. 1863-1870 ◽  
Author(s):  
P. Divieti ◽  
A. I. Geller ◽  
G. Suliman ◽  
H. Jüppner ◽  
F. R. Bringhurst
Keyword(s):  
Parathyroid Hormone ◽  
Ligand Binding ◽  
Terminal Region ◽  
Carboxyl Terminal

Parathyrin radioimmunoassay: diagnostic utility of antisera produced against carboxyl-terminal fragments of the hormone from the human.

1978 ◽  
Vol 24 (3) ◽  
pp. 451-454 ◽  
Author(s):  
F P Di Bella ◽  
J M Kehrwald ◽  
K Laakso ◽  
L Zitzner
Keyword(s):  
Renal Failure ◽  
Parathyroid Hormone ◽  
Chronic Renal Failure ◽  
Guinea Pigs ◽  
Normal Subjects ◽  
Terminal Region ◽  
Diagnostic Utility ◽  
Human Origin ◽  
Widespread Availability ◽  
Carboxyl Terminal

Abstract Antisera directed toward the carboxyl-terminal region of human parathyrin (parathyroid hormone), for use in daignostically applicable radioimmunoassays of the hormone in serum, are scarce, largely because of the lack of suitable immunogens of human origin. We produced four antisera in goats and guinea pigs by immunization with recently discovered carboxyl-terminal fragments of human parathyrin extracted from parathyroid tumors. Here, we report results of radioimmunoassays of nearly 200 normal and pathological sera with one of these antisera; we observed almost complete differentiation between concentrations of parathyrin in serum of healthy normal subjects and patients with primary, secondary (due to chronic renal failure), or "ectopic" hyperparathyroidism (due to nonparathyroid cancer). The availability of a new immunogen should now make possible the deliberate production of large quantities of diagnostically applicable parathyrin antisera directed toward the carboxyl-terminal region of human parathyrin. This should, in turn, lead to more widespread availability of this useful radioimmunoassay.

Comparison of two solid-phase peptide syntheses of a 32-amino acid carboxyl-terminal fragment of human parathyroid hormone, hPTH-(53–84)

1980 ◽  
Vol 199 (1) ◽  
pp. 286-296 ◽  
Author(s):  
Michael Rosenblatt ◽  
Geoffrey W. Tregear ◽  
Gary L. Shepard ◽  
George A. Tyler ◽  
Marta Veroni ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Amino Acid ◽  
Solid Phase ◽  
Human Parathyroid Hormone ◽  
Terminal Fragment ◽  
Carboxyl Terminal

Characterization of a novel parathyroid hormone (PTH) receptor with specificity for the carboxyl-terminal region of PTH-(1-84)

Endocrinology ◽  
1995 ◽  
Vol 136 (11) ◽  
pp. 4732-4740 ◽  
Author(s):  
N Inomata ◽  
M Akiyama ◽  
N Kubota ◽  
H Jüppner
Keyword(s):  
Parathyroid Hormone ◽  
Terminal Region ◽  
Carboxyl Terminal

Radioimmunoassay for the Middle Region of Human Parathyroid Hormone: Studies with a Radioiodinated Synthetic Peptide*

1981 ◽  
Vol 53 (1) ◽  
pp. 76-84 ◽  
Author(s):  
STEPHEN J. MARX ◽  
MARK E. SHARP ◽  
ADRIAN KRUDY ◽  
MICHAEL ROSENBLATT ◽  
LAWRENCE MALLETTE
Keyword(s):  
Parathyroid Hormone ◽  
Synthetic Peptide ◽  
Middle Region ◽  
Human Parathyroid Hormone

DEVELOPMENT OF HOMOLOGOUS IMMUNOLOGICAL ASSAYS FOR HUMAN PARATHYROID HORMONE

1980 ◽  
Vol 85 (1) ◽  
pp. 161-170 ◽  
Author(s):  
R. M. MANNING ◽  
G. N. HENDY ◽  
S. E. PAPAPOULOS ◽  
J. L. H. O'RIORDAN
Keyword(s):  
Parathyroid Hormone ◽  
Trichloroacetic Acid ◽  
Terminal Region ◽  
Human Parathyroid Hormone ◽  
Antibody Assay ◽  
Amino Terminal ◽  
High Affinity ◽  
Carboxy Terminal Region ◽  
Immunological Assays ◽  
Carboxy Terminal

SUMMARY Antisera to a trichloroacetic-acid precipitate of human parathyroid hormone (PTH) were produced in goats. Two of these antisera (G36 and G31) were of high affinity, and the bovine and porcine hormones were less reactive. Synthetic peptides containing the amino-terminal region of human PTH reacted with both antisera; the 1–34 peptide (PTH-(1–34)), with the sequence proposed by Niall, Sauer, Jacobs, Keutmann, Segre, O'Riordan, Aurbach & Potts in 1974, was more reactive than that having the sequence proposed by Brewer, Fairwell, Ronan, Sizemore & Arnaud in 1972. The antisera were further characterized with a number of other native and synthetic fragments of human PTH and reacted poorly with fragments from the carboxy-terminal region of the molecule. Since the amino-terminal fragments did not account for all the immunoreactivity, it is assumed that the antisera had some recognition sites for the central part of the molecule. Highly purified human PTH-(1–84) was labelled with 125I and radioimmunoassays were developed using this tracer and antiserum G36. To avoid the problems associated with labelling human PTH with 125I, a labelled antibody assay was developed with G36 and an immunoadsorbent consisting of human PTH-(1–34) (sequence of Niall et al.) coupled to cellulose. A sensitive homologous amino-terminal specific assay was developed in this way.

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