Abstract
With the growing recognition that all polypeptide hormones exist in heterogeneous forms, i.e., isohormones, this study represents the initial development of a comprehensive catalogue of the various isohormone species of human growth hormone (hGH) in relation to molecular structure. The catalogue is based primarily on results obtained in quantitative polyacrylamide gel electrophoresis (PAGE) in a multiphasic buffer system optimized for characterization of hGH. Thus, hGH forms can be recognized in objective, numerical terms based on physicochemical parameters of molecular size and net charge. Isoelectric focusing in polyacrylamide gel; and PAGE in sodium dodecyl sulphate in the presence and absence of reducing agents supplement the quantitative PAGE criteria. Spcific hGH immunoreactivity is necessary to completely distinguish hGH from hormones of similar size and charge properties (prolactin and chorionic somatomammotrophin). In the examination of eight standard hGH preparations obtained from four laboratories, all preparations exhibited multiple isohormone species, from two to five components per preparation. These identifiable components appear to represent the predominant species of a bidirectional continuum of hGH components, the continuum being in regard to both molecular size and charge. Within any given preparations, the continuum presents itself as a series of identifiable 'charge isomers'. Between preparations, in addition, there are size differences which may relate to conformational changes (unfolding) in some preparations.
| Original language | English |
|---|---|
| Journal | Acta Endocrinologica, Supplement |
| Volume | 85 |
| Issue number | sup 211 |
| State | Published - Dec 1 1977 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Endocrinology
Cite this
A catalogue of isohormones of human growth hormone based on quantitative polyacrylamide gel electrophoresis. / Skyler, Jay S; Baumann, G.; Chrambach, A.
In: Acta Endocrinologica, Supplement, Vol. 85, No. sup 211, 01.12.1977.Research output: Contribution to journal › Article
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TY - JOUR
T1 - A catalogue of isohormones of human growth hormone based on quantitative polyacrylamide gel electrophoresis
AU - Skyler, Jay S
AU - Baumann, G.
AU - Chrambach, A.
PY - 1977/12/1
Y1 - 1977/12/1
N2 - With the growing recognition that all polypeptide hormones exist in heterogeneous forms, i.e., isohormones, this study represents the initial development of a comprehensive catalogue of the various isohormone species of human growth hormone (hGH) in relation to molecular structure. The catalogue is based primarily on results obtained in quantitative polyacrylamide gel electrophoresis (PAGE) in a multiphasic buffer system optimized for characterization of hGH. Thus, hGH forms can be recognized in objective, numerical terms based on physicochemical parameters of molecular size and net charge. Isoelectric focusing in polyacrylamide gel; and PAGE in sodium dodecyl sulphate in the presence and absence of reducing agents supplement the quantitative PAGE criteria. Spcific hGH immunoreactivity is necessary to completely distinguish hGH from hormones of similar size and charge properties (prolactin and chorionic somatomammotrophin). In the examination of eight standard hGH preparations obtained from four laboratories, all preparations exhibited multiple isohormone species, from two to five components per preparation. These identifiable components appear to represent the predominant species of a bidirectional continuum of hGH components, the continuum being in regard to both molecular size and charge. Within any given preparations, the continuum presents itself as a series of identifiable 'charge isomers'. Between preparations, in addition, there are size differences which may relate to conformational changes (unfolding) in some preparations.
AB - With the growing recognition that all polypeptide hormones exist in heterogeneous forms, i.e., isohormones, this study represents the initial development of a comprehensive catalogue of the various isohormone species of human growth hormone (hGH) in relation to molecular structure. The catalogue is based primarily on results obtained in quantitative polyacrylamide gel electrophoresis (PAGE) in a multiphasic buffer system optimized for characterization of hGH. Thus, hGH forms can be recognized in objective, numerical terms based on physicochemical parameters of molecular size and net charge. Isoelectric focusing in polyacrylamide gel; and PAGE in sodium dodecyl sulphate in the presence and absence of reducing agents supplement the quantitative PAGE criteria. Spcific hGH immunoreactivity is necessary to completely distinguish hGH from hormones of similar size and charge properties (prolactin and chorionic somatomammotrophin). In the examination of eight standard hGH preparations obtained from four laboratories, all preparations exhibited multiple isohormone species, from two to five components per preparation. These identifiable components appear to represent the predominant species of a bidirectional continuum of hGH components, the continuum being in regard to both molecular size and charge. Within any given preparations, the continuum presents itself as a series of identifiable 'charge isomers'. Between preparations, in addition, there are size differences which may relate to conformational changes (unfolding) in some preparations.
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M3 - Article
VL - 85
JO - European Journal of Endocrinology
JF - European Journal of Endocrinology
SN - 0804-4643
IS - sup 211
ER -