outside the plasma membrane (Wang et al. 2002). Based on the sequence similarity of the
rabbit and human GHRs in the extracellular stem region, it appears likely that the human …

Two growth hormone-binding proteins (GH-BPS) have recently been discovered in human
plasma. Both are specific for human GH; one has high afjkity and the other has low afinity …

In our previous description of the circulating GH-binding protein (GH-BP) we observed, in
addition to the main GH-BP complex, a second macromolecular component designated …

The recent demonstration of two independent receptor-binding sites (sites 1 and 2) on
human GH (hGH) raises the question of the stoichiometry of circulating GH-binding protein …

Conclusions The recognition of circulating GHBP has added a new element of complexity to
the GH-IGF axis. At the same time, it has facilitated investigation of that axis. The nature of …

Human serum contains a high affinity GHbinding protein (GHBP) whose amino-terminal
sequence is identical to the extracellular domain of the GH receptor. Current methods that …

In most species, the structure of the growth hormone-binding protein (GH-BP) is identical to
that of the growth hormone receptor (GH-R). The affinity (Ka) of the GH-BP is however 10 x …

The recent discovery of a GH-binding protein (GH-BP) in human serum has important
implications for the distribution, metabolism, and physiological activity of human GH (hGH) …

GH specifically interacts with a soluble binding protein in serum. The GH-binding protein
(GHBP) has been shown to contain the extracellular portion of the cell surface GH receptor …

GH forms a high Mr complex in rat serum distinct from that with GH-binding protein (GHBP).
The present study investigates the nature of this complex. When subjected to AcA44 filtration …