What question did this study set out to answer?

To purify and characterize 22,000-mol.wt. human somatotropin and its 20,000-mol.wt. variant, evaluating their specific binding properties to rabbit liver and mammary-gland receptors.

September 15, 1983Biochemical JournalOpen Access

Purification of the 22000- and 20000-mol.wt. forms of human somatotropin and characterization of their binding to liver and mammary binding sites

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Authors

JCJean ClossetErasmus Hospital JSJean SmalCity Of Hope National Medical Center FGFulgencio GómezComplejo Asistencial Universitario de Palencia

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Implication

Biochemical analysis demonstrates distinct binding capacities of 22-kDa and 20-kDa human somatotropin in rabbit tissues, indicating both act as partial agonists.

Key Points

To purify and characterize 22,000-mol.wt. human somatotropin and its 20,000-mol.wt. variant, evaluating their specific binding properties to rabbit liver and mammary-gland receptors.
Purified and chemically characterized 22,000-mol.wt. somatotropin and its 20,000-mol.wt. variant, verifying variant contamination was 0.5% by weight using a monoclonal antibody radioimmunoassay.
Radiolabeled both hormone forms with 125I using the Iodogen method and assessed binding parameters across pregnant-rabbit liver particulate and mammary-gland receptor preparations.
Maximum binding capacity of 125I-labeled somatotropin to liver particulate receptor was 50% to 60%, whereas the 20,000-mol.wt. variant achieved 30% binding capacity.
Affinity constants and binding capacities were 0.7 x 10^10 M^-1 and 815 fmol/mg of protein for 22,000-mol.wt. somatotropin, compared to 0.6 x 10^10 M^-1 and 1,250 fmol/mg of protein for the 20,000-mol.wt. variant.

Cite This Study

Closset et al. (1983) studied this question.

synapsesocial.com/papers/6a89b81f5c4c6b099dec7ddc https://doi.org/10.1042/bj2140885

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Implication

Biochemical analysis demonstrates distinct binding capacities of 22-kDa and 20-kDa human somatotropin in rabbit tissues, indicating both act as partial agonists.

Purification of the 22000- and 20000-mol.wt. forms of human somatotropin and characterization of their binding to liver and mammary binding sites

Discussion

Member takes

Implication

Key Points

Cite This Study

Purification of the 22000- and 20000-mol.wt. forms of human somatotropin and characterization of their binding to liver and mammary binding sites

Discussion

Member takes

Implication

Key Points

Cite This Study

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