Solubilization of a parathyroid hormone receptor from bovine kidney cortex plasma membranes

Craig C. Malbon; James E. Zull

doi:10.1016/S0006-291X(75)80311-1

Solubilization of a parathyroid hormone receptor from bovine kidney cortex plasma membranes

Craig C. Malbon
, James E. Zull

Pharmacological Sciences

Stony Brook University

Case Western Reserve University

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Preparation of a soluble extract of bovine kidney cortex plasma membranes with Triton X-100 is described. Interaction of this extract with tritiated parathyroid hormone was detected using three distinct binding assays: gel filtration chromatography, precipitation of bound hormone with polyethylene glycol, and adsorption of free hormone with microfine silica. The binding of parathyroid hormone to the component(s) in the extract was highly specific and sensitive to competition by purified native parathyroid hormone and synthetic (1-34) bovine parathyroid hormone. Inactivation of the tritiated parathyroid hormone by oxidation led to loss of its binding activity.

Original language	English
Pages (from-to)	179-187
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	66
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(75)80311-1
State	Published - Sep 2 1975

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title = "Solubilization of a parathyroid hormone receptor from bovine kidney cortex plasma membranes",

abstract = "Preparation of a soluble extract of bovine kidney cortex plasma membranes with Triton X-100 is described. Interaction of this extract with tritiated parathyroid hormone was detected using three distinct binding assays: gel filtration chromatography, precipitation of bound hormone with polyethylene glycol, and adsorption of free hormone with microfine silica. The binding of parathyroid hormone to the component(s) in the extract was highly specific and sensitive to competition by purified native parathyroid hormone and synthetic (1-34) bovine parathyroid hormone. Inactivation of the tritiated parathyroid hormone by oxidation led to loss of its binding activity.",

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AU - Zull, James E.

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N2 - Preparation of a soluble extract of bovine kidney cortex plasma membranes with Triton X-100 is described. Interaction of this extract with tritiated parathyroid hormone was detected using three distinct binding assays: gel filtration chromatography, precipitation of bound hormone with polyethylene glycol, and adsorption of free hormone with microfine silica. The binding of parathyroid hormone to the component(s) in the extract was highly specific and sensitive to competition by purified native parathyroid hormone and synthetic (1-34) bovine parathyroid hormone. Inactivation of the tritiated parathyroid hormone by oxidation led to loss of its binding activity.

AB - Preparation of a soluble extract of bovine kidney cortex plasma membranes with Triton X-100 is described. Interaction of this extract with tritiated parathyroid hormone was detected using three distinct binding assays: gel filtration chromatography, precipitation of bound hormone with polyethylene glycol, and adsorption of free hormone with microfine silica. The binding of parathyroid hormone to the component(s) in the extract was highly specific and sensitive to competition by purified native parathyroid hormone and synthetic (1-34) bovine parathyroid hormone. Inactivation of the tritiated parathyroid hormone by oxidation led to loss of its binding activity.

UR - https://www.scopus.com/pages/publications/0016719036

U2 - 10.1016/S0006-291X(75)80311-1

DO - 10.1016/S0006-291X(75)80311-1

M3 - Article

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SP - 179

EP - 187

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 1

ER -

Solubilization of a parathyroid hormone receptor from bovine kidney cortex plasma membranes

Abstract

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