I. Jonsdottir et al., HIGH-MOLECULAR-WEIGHT GROWTH-HORMONE (GREATER-THAN-160 KD) IN HUMAN SERUM CHARACTERIZED WITH MONOCLONAL-ANTIBODIES, Hormone research, 41(5-6), 1994, pp. 197-204
Human growth hormone (hGH) was analyzed by six monoclonal antibodies (
Mabs) and a polyclonal antiserum (Pas) before and after molecular siev
e 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 reacte
d with five distinct epitopes and bound to a hGH fragment correspondin
g to the amino acid sequence 15-125. Two of the Mabs showed reduced bi
nding 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 P
as 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 det
ected the hGH immunoreactivity (>160 kD) in a similar manner. This hig
h molecular weight hGH (>160 M)) was distinguishable from the identifi
ed, receptor-like hGH-binding protein in serum.