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

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

3 Citas (Scopus)

Resumen

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.

Idioma original	English
Páginas (desde-hasta)	596-603
Número de páginas	8
Publicación	Biochemical and Biophysical Research Communications
Volumen	139
N.º	2
DOI	https://doi.org/10.1016/S0006-291X(86)80032-8
Estado	Published - sep. 16 1986
Publicado de forma externa	Sí

Nota bibliográfica

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

Acceder al documento

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

Otros archivos y enlaces

Citar esto

@article{ef3d535e39c24951bc46b2751fd1eb34,

title = "Identification of a major bovine heart Ca2+ binding protein",

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,",

year = "1986",

month = sep,

day = "16",

doi = "10.1016/S0006-291X(86)80032-8",

language = "English",

volume = "139",

pages = "596--603",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Identification of a major bovine heart Ca2+ binding protein

AU - Waisman, David Morton

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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0022465968&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022465968&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(86)80032-8

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

M3 - Article

C2 - 3767980

AN - SCOPUS:0022465968

SN - 0006-291X

VL - 139

SP - 596

EP - 603

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -