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High molecular weight growth hormone (> 160 kD) in human serum characterized with monoclonal antibodies

Study · human · Hormone research · 1994 · DOI 10.1159/000183892 · PMID 7525441

Plain-language summary

Paraphrased from the published abstract below — not a verdict on whether anything works.

This human study analyzed serum samples from healthy subjects for high molecular weight human growth hormone (hGH) using six monoclonal antibodies (Mabs) and a polyclonal antiserum (Pas), before and after molecular sieve chromatography. Baseline hGH levels measured with Pas were between < 0.2 and 0.4 ng/ml; the six Mabs, reacting with five distinct epitopes and binding an hGH fragment corresponding to amino acids 15-125, measured unfractionated serum hGH levels of < 3.1-390 ng/ml, with two Mabs showing reduced binding to 20-kD hGH. After chromatography, one peak of hGH-immunoreactive material above 160 kD and one at the monomeric hGH elution volume were detected with both Pas and Mabs; the high molecular weight peak appeared to consist mainly of 22-kD hGH molecules and was distinguishable from a previously identified hGH-binding protein.

Abstract

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.

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