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Related Experiment Videos

A second, lower affinity growth hormone-binding protein in human plasma.

G Baumann1, M A Shaw

  • 1Department of Medicine, Northwestern University Medical School, Chicago, Illinois 60611.

The Journal of Clinical Endocrinology and Metabolism
|March 1, 1990
PubMed
Summary

Researchers identified a second growth hormone-binding protein (GH-BP) complex, termed peak I, characterized by low affinity binding to GH. This finding expands our understanding of GH-BP interactions in plasma.

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Area of Science:

  • Endocrinology
  • Protein Chemistry
  • Biochemistry

Background:

  • Previous studies identified a primary growth hormone-binding protein (GH-BP) complex.
  • A secondary component, peak I, was observed but not fully characterized due to its low magnitude and apparent nonsaturability.

Purpose of the Study:

  • To characterize the nature of the previously observed peak I component.
  • To determine if peak I represents a distinct GH-binding protein (GH-BP) complex.

Main Methods:

  • Incubation of plasma or isolated peak I-BP with monomeric [125I]GH and varying concentrations of unlabeled GH.
  • Analysis by Sephadex G-100 chromatography to separate bound and free GH.
  • Characterization of cross-linked GH-peak I BP complexes using SDS-PAGE, isoelectric focusing, and 2D electrophoresis.

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Main Results:

  • Peak I binding of GH was found to be saturable with human GH but not with animal GHs.
  • Saturation/Scatchard analysis indicated a low affinity association constant (10^5 M-1) and a binding capacity of 15 mg/L plasma.
  • Cross-linked peak I complexes exhibited a molecular weight of 124 kD and a pI of 7, distinct from the high-affinity GH-BP complex (76 kD, pI 5).

Conclusions:

  • Peak I represents a low-affinity GH-binding protein (GH-BP) complex.
  • This low-affinity GH-BP complex is distinct from the previously described high-affinity GH-BP complex.
  • The characterization of peak I provides a more comprehensive understanding of GH-BP heterogeneity in plasma.