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PURIFICATION OF HUMAN PARATHYROID HORMONE: RECENT STUDIES AND FURTHER OBSERVATIONS

PURIFICATION OF HUMAN PARATHYROID HORMONE: RECENT STUDIES AND FURTHER OBSERVATIONS During the isolation of human parathyroid hormone there is an extensive loss of immunoassayable hormone over the successive extraction steps, due in part to the presence of fragments that are soluble in 4% trichloroacetic acid. These fragments are derived from both the amino- and carboxyl-terminal regions of the hormone.The hormonal fractions precipitated with trichloroacetic acid were further purified by gel filtration and ion-exchange chromatography. At the final ion-exchange purification step, some preparations of the hormone eluted in multiple fractions. When the various components were characterized separately by immunoassay, amino acid composition, enzymic cleavage and partial sequence analysis, they were found to be closely comparable, although the most acidic fraction contained a blocked terminal amino group.Extraction of a number of batches of tissue permitted revision of the amino acid composition of human parathyroid hormone. Biosynthetic studies with labelled amino acids confirmed the absence of tyrosine and the presence of phenylalanine and threonine and localized these residues to definite regions of the molecule. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Endocrinology Bioscientifica

PURIFICATION OF HUMAN PARATHYROID HORMONE: RECENT STUDIES AND FURTHER OBSERVATIONS

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Publisher
Bioscientifica
Copyright
Copyright © 1978 The Authors. All Rights Reserved.
ISSN
0022-0795
eISSN
1479-6805
DOI
10.1677/joe.0.0780049
Publisher site
See Article on Publisher Site

Abstract

During the isolation of human parathyroid hormone there is an extensive loss of immunoassayable hormone over the successive extraction steps, due in part to the presence of fragments that are soluble in 4% trichloroacetic acid. These fragments are derived from both the amino- and carboxyl-terminal regions of the hormone.The hormonal fractions precipitated with trichloroacetic acid were further purified by gel filtration and ion-exchange chromatography. At the final ion-exchange purification step, some preparations of the hormone eluted in multiple fractions. When the various components were characterized separately by immunoassay, amino acid composition, enzymic cleavage and partial sequence analysis, they were found to be closely comparable, although the most acidic fraction contained a blocked terminal amino group.Extraction of a number of batches of tissue permitted revision of the amino acid composition of human parathyroid hormone. Biosynthetic studies with labelled amino acids confirmed the absence of tyrosine and the presence of phenylalanine and threonine and localized these residues to definite regions of the molecule.

Journal

Journal of Endocrinology – Bioscientifica

Published: Jul 1, 1978

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