Identification of a major bovine heart Ca2+ binding protein

David Morton Waisman; Navin C. Khanna; Masaaki Tokuda

doi:10.1016/S0006-291X(86)80032-8

Identification of a major bovine heart Ca²⁺ binding protein

David Morton Waisman, Navin C. Khanna, Masaaki Tokuda

Résultat de recherche: Article › examen par les pairs

3 Citations (Scopus)

Résumé

The 100,000 × g supernatant of bovine heart has been chromatographed on DEAE-cellulose and the resultant fractions have been analyzed for both calcium binding activity and calmodulin activity. Of the four peaks of calcium binding activity detected by this procedure only a single peak (peak IV) was identified as calmodulin. The calcium binding activity of the largest peak (peak III) has been subjected to further purification and a single calcium binding protein of M_r 63,000 isolated. Biochemical and immunological results documented that the 63 kDa protein is identical to calregulin. The results of this study identify calregulin as a major bovine heart calcium binding protein.

Langue d'origine	English
Pages (de-à)	596-603
Nombre de pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	139
Numéro de publication	2
DOI	https://doi.org/10.1016/S0006-291X(86)80032-8
Statut de publication	Published - sept. 16 1986
Publié à l'externe	Oui

Note bibliographique

Funding Information:
-Supported by a grant from the Alberta Heart Foundation (DMW) and the Alberta Heritage Foundation for Medical Research (NCK and MT). *To whom all correspondence should be addressed. Abbreviations: HPLC, High performance liquid chromatography; DTT, Dithioerythritol; DEAE, Diethylaminoethyl; MOPS, 3-(N-morpholino) propanesulfonic acid,

ASJC Scopus Subject Areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Accès au document

10.1016/S0006-291X(86)80032-8

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abstract = "The 100,000 × g supernatant of bovine heart has been chromatographed on DEAE-cellulose and the resultant fractions have been analyzed for both calcium binding activity and calmodulin activity. Of the four peaks of calcium binding activity detected by this procedure only a single peak (peak IV) was identified as calmodulin. The calcium binding activity of the largest peak (peak III) has been subjected to further purification and a single calcium binding protein of Mr 63,000 isolated. Biochemical and immunological results documented that the 63 kDa protein is identical to calregulin. The results of this study identify calregulin as a major bovine heart calcium binding protein.",

author = "Waisman, {David Morton} and Khanna, {Navin C.} and Masaaki Tokuda",

note = "Funding Information: -Supported by a grant from the Alberta Heart Foundation (DMW) and the Alberta Heritage Foundation for Medical Research (NCK and MT). *To whom all correspondence should be addressed. Abbreviations: HPLC, High performance liquid chromatography; DTT, Dithioerythritol; DEAE, Diethylaminoethyl; MOPS, 3-(N-morpholino) propanesulfonic acid,",

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AU - Khanna, Navin C.

AU - Tokuda, Masaaki

N1 - Funding Information: -Supported by a grant from the Alberta Heart Foundation (DMW) and the Alberta Heritage Foundation for Medical Research (NCK and MT). *To whom all correspondence should be addressed. Abbreviations: HPLC, High performance liquid chromatography; DTT, Dithioerythritol; DEAE, Diethylaminoethyl; MOPS, 3-(N-morpholino) propanesulfonic acid,

PY - 1986/9/16

Y1 - 1986/9/16

N2 - The 100,000 × g supernatant of bovine heart has been chromatographed on DEAE-cellulose and the resultant fractions have been analyzed for both calcium binding activity and calmodulin activity. Of the four peaks of calcium binding activity detected by this procedure only a single peak (peak IV) was identified as calmodulin. The calcium binding activity of the largest peak (peak III) has been subjected to further purification and a single calcium binding protein of Mr 63,000 isolated. Biochemical and immunological results documented that the 63 kDa protein is identical to calregulin. The results of this study identify calregulin as a major bovine heart calcium binding protein.

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