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      High Molecular Weight Growth Hormone ( > 160 kD) in Human Serum Characterized with Monoclonal Antibodies

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          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-immuno-reactive 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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          Author and article information

          Journal
          HRE
          Horm Res Paediatr
          10.1159/issn.1663-2818
          Hormone Research in Paediatrics
          S. Karger AG
          1663-2818
          1663-2826
          1994
          1994
          05 December 2008
          : 41
          : 5-6
          : 197-204
          Affiliations
          aDepartment of Immunology, University of Stockholm, Stockholm, Sweden; bDepartment of Immunology, National University Hospital, Landspítalinn, Reykjavik, Iceland; cDepartment of Endocrinology, Karolinska Institute, Stockholm, dResearch and Development, Kabi Pharmacia, Stockholm, and eDepartment of Biochemistry, Biomedical Centre, University of Uppsala, Sweden
          Article
          183892 Horm Res 1994;41:197–204
          10.1159/000183892
          7525441
          © 1994 S. Karger AG, Basel

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          Page count
          Pages: 8
          Categories
          Original Paper

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