Growth Hormone Production by Human Pituitary Glands in Organ Culture: Evidence for Predominant Secretion of the Single-Chain 22,000 Molecular Weight Form (Isohormone B)*

Baumann, Gerhard; Maccart, John G.

doi:10.1210/jcem-55-4-611

Cited by 34 publications

(7 citation statements)

References 31 publications

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“…PAGE was performed in the presence of SDS with and without sulfhydryl reduction (10 mM DTT) in 10% T (total monomer), 2% C (cross-linked) gel slabs (9.98% acrylamide-0.02% N,iV'-methylene bisacrylamide) in a glycine-chlorideAmmediol buffer system operating at pH 9.6, described in detail previously (12). IF was carried out at 400 V in 5% T, 2% C gel slabs at 0 C for 7 h in the presence of 2% carrier ampholytes (Pharmalyte; nominal pi 3-10).…”

Section: Polyacrylamide Gel Electrophoresis (Page) and Isoelectric Fomentioning

confidence: 99%

A Second, Lower Affinity Growth Hormone-Binding Protein in Human Plasma*

Baumann

Shaw

1990

The Journal of Clinical Endocrinology & Metabolism

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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 peak I during gel filtration of [125I]GH-plasma mixtures. This component was not further characterized because of its small magnitude, seeming nonsaturability, and suspected artifactual nature. We have now characterized peak I as the complex of a low affinity BP with GH. To gain a better knowledge of the nature of peak I, whole plasma or plasma fractions containing isolated peak I-BP (ammonium sulfate precipitated or prepared by gel filtration of plasma) were incubated with monomeric [125I]GH and varying concentrations of unlabeled GH. The mixtures were then analyzed by Sephadex G-100 chromatography to separate free from protein-bound GH. Peak I-associated radioactivity was saturable at high concentrations of human GH, but not with animal GHs. Saturation/Scatchard analysis yielded an association constant of 10(5) M-1 and a maximum binding capacity of 15 mg/L plasma. Chemically cross-linked complexes of [125I]GH with isolated peak I BP were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, isoelectric focusing, and two-dimensional electrophoresis. These experiments yielded a mol wt of 124 kD and a pI of 7 for the cross-linked complex. This is in contradistinction to the previously reported high affinity GH-BP complex, which when cross-linked has a mol wt of 76 kD and a pI of 5.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Polyacrylamide Gel Electrophoresis (Page) and Isoelectric Fomentioning

confidence: 99%

A Second, Lower Affinity Growth Hormone-Binding Protein in Human Plasma*

Baumann

Shaw

1990

The Journal of Clinical Endocrinology & Metabolism

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100

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“…Secreted forms of GH. GH variants that are secreted in vitro include 22 kDa, 20 kDa, deamidated and acylated GH (5,6,33). as well as GH oligomers ( 5 , 34,35).…”

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confidence: 99%

Growth Hormone Binding Proteins and Various Forms of Growth Hormone: Implications for Measurements

Baumann

1990

Acta Paediatrica

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“…These figures are based on a composite of data from pituitary extracts [10,11,19,71,91] and GH isoforms released by pituitary cultures in vitro [92][93][94][95]. The proportion of extraction artifacs (e.g.…”

Section: Proportions Of Gh Isoforms In the Pituitarymentioning

confidence: 99%