PROPERTIES OF ANTISERA AGAINST SYNTHETIC 1–34 HUMAN PARATHYROID HORMONE

in Journal of Endocrinology
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T. J. VISSER
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C. J. BUURMAN
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W. H. L. HACKENG
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J. C. BIRKENHÄGER
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Department of Internal Medicine III and Clinical Endocrinology, Medical Faculty, Erasmus University, Rotterdam, and * Laboratory ofEndocrinological Chemistry, Municipal Hospital 'Bergweg', Rotterdam, The Netherlands

(Received 2 June 1975)

The availability of synthetic human parathyroid hormone (hPTH) fragments (Andreatta, Hartmann, Jöhl, Kamber, Maier, Riniker, Rittel & Sieber, 1973; Tregear, Van Rietschoten, Greene, Niall, Keutmann, Parsons, O'Riordan & Potts, 1974) has enabled the production of region specific antibodies and thus the development of region specific radioimmunoassays (RIA). This is particularly meaningful with respect to the heterogeneity of immunoreactive forms of PTH in the circulation (Arnaud, Goldsmith, Bordier, Sizemore, Larsen & Gilkinson, 1974). The peptides were synthesized according to the sequences proposed for the first 34 amino acids by Brewer, Fairwell, Ronan, Sizemore & Arnaud (1972) (referred to as 1–34 hPTH-B) and Niall, Sauer, Jacobs, Keutmann, Segre, O'Riordan, Aurbach & Potts (1974) (1–34 hPTH-N), which differ in positions 22, 28 and 30.

Two

 

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