Nuclear matrix as acceptor for cAMP-binding proteins

Said A. Goueli; Khalil Ahmed

doi:10.1016/0006-291X(82)91887-3

Nuclear matrix as acceptor for cAMP-binding proteins

Said A. Goueli, Khalil Ahmed

Laboratory Medicine and Pathology

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

4 Scopus citations

Abstract

Using [³²P]-8-N₃-cAMP, a photoaffinity analog of cAMP, we have established that nuclear binding of cAMP is preferentially localized in the "nuclear matrix". Two major radioactive bands corresponded to proteins of M_r 40 K and 50 K, and three minor bands to proteins of M_r 55, 150 and 200 K. Even though the molecular weight of the major nuclear binding proteins in the matrix are similar to those of the cytosolic cAMP binding proteins, the characteristics of the binding reaction in the nucleus were markedly different from those in the cytosol.

Original language	English (US)
Pages (from-to)	1083-1088
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	109
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(82)91887-3
State	Published - Dec 31 1982

Bibliographical note

Funding Information:
in part by funds from the V.A. grant CA-15062 from National Cancer Mr. Alan Davis for his help in this

Funding Information:
Acknowledgments: This work is supported Medical Research Fund, and by research Institute, D.H.H.S., P.H.S. We thank work.

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10.1016/0006-291X(82)91887-3

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title = "Nuclear matrix as acceptor for cAMP-binding proteins",

abstract = "Using [32P]-8-N3-cAMP, a photoaffinity analog of cAMP, we have established that nuclear binding of cAMP is preferentially localized in the {"}nuclear matrix{"}. Two major radioactive bands corresponded to proteins of Mr 40 K and 50 K, and three minor bands to proteins of Mr 55, 150 and 200 K. Even though the molecular weight of the major nuclear binding proteins in the matrix are similar to those of the cytosolic cAMP binding proteins, the characteristics of the binding reaction in the nucleus were markedly different from those in the cytosol.",

author = "Goueli, {Said A.} and Khalil Ahmed",

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AU - Goueli, Said A.

AU - Ahmed, Khalil

N1 - Funding Information: in part by funds from the V.A. grant CA-15062 from National Cancer Mr. Alan Davis for his help in this Funding Information: Acknowledgments: This work is supported Medical Research Fund, and by research Institute, D.H.H.S., P.H.S. We thank work.

PY - 1982/12/31

Y1 - 1982/12/31

N2 - Using [32P]-8-N3-cAMP, a photoaffinity analog of cAMP, we have established that nuclear binding of cAMP is preferentially localized in the "nuclear matrix". Two major radioactive bands corresponded to proteins of Mr 40 K and 50 K, and three minor bands to proteins of Mr 55, 150 and 200 K. Even though the molecular weight of the major nuclear binding proteins in the matrix are similar to those of the cytosolic cAMP binding proteins, the characteristics of the binding reaction in the nucleus were markedly different from those in the cytosol.

AB - Using [32P]-8-N3-cAMP, a photoaffinity analog of cAMP, we have established that nuclear binding of cAMP is preferentially localized in the "nuclear matrix". Two major radioactive bands corresponded to proteins of Mr 40 K and 50 K, and three minor bands to proteins of Mr 55, 150 and 200 K. Even though the molecular weight of the major nuclear binding proteins in the matrix are similar to those of the cytosolic cAMP binding proteins, the characteristics of the binding reaction in the nucleus were markedly different from those in the cytosol.

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JF - Biochemical and Biophysical Research Communications

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ER -

Nuclear matrix as acceptor for cAMP-binding proteins

Abstract

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