Characterization of gingival epithelium epidermal growth factor receptor

S. Sengupta; J. Liu; S. L. Wang; E. Piotrowski; A. Slomiany; B. L. Slomiany

Characterization of gingival epithelium epidermal growth factor receptor

S. Sengupta
, J. Liu
, S. L. Wang
, E. Piotrowski
, A. Slomiany
, B. L. Slomiany

School of Dental Medicine, Oral Biology

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

Abstract

The binding characteristics of gingival epithelium epidermal growth factor (EGF) receptor were investigated using epithelial cell membranes from bovine gingiva. The binding of [¹²⁵I]EGF was found to be time and protein concentration dependent, reversible, and specific. Unlabeled EGF competed for [¹²⁵I]EGF binding with IC₅₀ of 0.25nM and maximum displacement of 93% at 0.81nM. Scatchard analysis of the binding data inferred the presence of two binding sites, one of high affinity (Kd=3.3nM and B(max)=47.3fmol/mg protein) and the other of a low affinity (Kd=1.6μM and B(max)=1.9pmol/mg protein). Crosslinking of [¹²⁵I]EGF to gingival membranes followed by polyacrylamide gel electrophoresis and autoradiography revealed a receptor protein of 170kDa.

Original language	English (US)
Pages (from-to)	335-342
Number of pages	8
Journal	Biochemistry International
Volume	23
Issue number	2
State	Published - 1991

All Science Journal Classification (ASJC) codes

Biochemistry

Cite this

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title = "Characterization of gingival epithelium epidermal growth factor receptor",

abstract = "The binding characteristics of gingival epithelium epidermal growth factor (EGF) receptor were investigated using epithelial cell membranes from bovine gingiva. The binding of [125I]EGF was found to be time and protein concentration dependent, reversible, and specific. Unlabeled EGF competed for [125I]EGF binding with IC50 of 0.25nM and maximum displacement of 93\% at 0.81nM. Scatchard analysis of the binding data inferred the presence of two binding sites, one of high affinity (Kd=3.3nM and B(max)=47.3fmol/mg protein) and the other of a low affinity (Kd=1.6μM and B(max)=1.9pmol/mg protein). Crosslinking of [125I]EGF to gingival membranes followed by polyacrylamide gel electrophoresis and autoradiography revealed a receptor protein of 170kDa.",

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journal = "Biochemistry International",

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T1 - Characterization of gingival epithelium epidermal growth factor receptor

AU - Sengupta, S.

AU - Liu, J.

AU - Wang, S. L.

AU - Piotrowski, E.

AU - Slomiany, A.

AU - Slomiany, B. L.

PY - 1991

Y1 - 1991

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AB - The binding characteristics of gingival epithelium epidermal growth factor (EGF) receptor were investigated using epithelial cell membranes from bovine gingiva. The binding of [125I]EGF was found to be time and protein concentration dependent, reversible, and specific. Unlabeled EGF competed for [125I]EGF binding with IC50 of 0.25nM and maximum displacement of 93% at 0.81nM. Scatchard analysis of the binding data inferred the presence of two binding sites, one of high affinity (Kd=3.3nM and B(max)=47.3fmol/mg protein) and the other of a low affinity (Kd=1.6μM and B(max)=1.9pmol/mg protein). Crosslinking of [125I]EGF to gingival membranes followed by polyacrylamide gel electrophoresis and autoradiography revealed a receptor protein of 170kDa.

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JO - Biochemistry International

JF - Biochemistry International

IS - 2

ER -

Characterization of gingival epithelium epidermal growth factor receptor

Abstract

All Science Journal Classification (ASJC) codes

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