| Autor: |
Jónsdóttir I; Department of Immunology, University of Stockholm, Sweden., Luthman M, Ekre HP, Skoog B, Brostedt P, Roos P, Werner S, Perlmann P |
| Jazyk: |
angličtina |
| Zdroj: |
Hormone research [Horm Res] 1994; Vol. 41 (5-6), pp. 197-204. |
| DOI: |
10.1159/000183892 |
| Abstrakt: |
Human growth hormone (hGH) was analyzed by six monoclonal antibodies (Mabs) and a polyclonal antiserum (Pas) before and after molecular sieve chromatography of sera from healthy subjects. Their hGH levels were between < 0.2 and 0.4 ng/ml as determined with Pas. The six Mabs reacted with five distinct epitopes and bound to a hGH fragment corresponding to the amino acid sequence 15-125. Two of the Mabs showed reduced binding to 20-kD hGH. The binding of Mabs to dimeric forms of hGH varied. Human GH levels in unfractionated sera as determined with Mabs were < 3.1-390 ng/ml. After molecular sieve chromatography of the sera, one peak of hGH-immunoreactive material of high molecular weight (> 160 kD) and one at the elution volume of monomeric hGH were determined with Pas and Mabs. The major part of the high molecular weight hGH (> 160 kD) seemed to consist of 22-kD hGH molecules, since Pas and all Mabs detected the hGH immunoreactivity (> 160 kD) in a similar manner. This high molecular weight hGH (> 160 kD) was distinguishable from the identified, receptor-like hGH-binding protein in serum. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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