Growth hormone-binding proteins of human serum: developmental patterns in normal man

1992 ◽  
Vol 75 (3) ◽  
pp. 852-854 ◽  
Author(s):  
T. J. Merimee
1993 ◽  
Vol 129 (6) ◽  
pp. 559-564 ◽  
Author(s):  
Guy Massa ◽  
Mapoko Ilondo ◽  
Magda Vanderschueren-Lodeweyckx

The characteristics of the human serum growth hormone-binding protein (GHBP) were compared with those of a water-soluble GH-binding site prepared by incubating cultured IM-9 lymphocytes in assay buffer with 25 mmol/l iodoacetamide. High-performance liquid chromatography gel filtration of the water-soluble GH-binding site incubated with 125I-labeled human GH ([125I]hGH) revealed a large peak of bound [125I]hGH eluting at the same position as the peak of [125I]hGH bound to the GHBP in serum. The estimated Mr of the peak was 120 000, presumably representing one [125I]hGH bound to two binding sites. The binding specificities of the serum GHBP, the water-soluble GH-binding site and the GH receptor on IM-9 lymphocytes were identical. The binding affinities for 22 000 hGH and for 20 000 hGH of the serum GHBP were similar to the binding affinity of the water-soluble GH-binding site but lower than those of the cellular GH receptor. These findings show that the characteristics of the serum GHBP are comparable to those of the water-soluble GH-binding site released from IM-9 cells and support the hypothesis that in man the serum GHBP is produced by proteolytic cleavage of the cellular GH receptor.


1986 ◽  
Vol 881 (2) ◽  
pp. 236-240 ◽  
Author(s):  
Adrian C. Herington ◽  
Susie Ymer ◽  
Peter Roupas ◽  
Janet Stevenson

1989 ◽  
Vol 3 (8) ◽  
pp. 1173-1182 ◽  
Author(s):  
Annette Møldrup ◽  
Nils Billestrup ◽  
Niels A. Thorn ◽  
Åke Lernmark ◽  
Jens Høiriis Nielsen

1992 ◽  
Vol 32 (1) ◽  
pp. 69-72 ◽  
Author(s):  
Guy Massa ◽  
Francis de Zegher ◽  
Magda Vanderschueren-Lodeweyckx

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