Comparison of two calcium-dependent proteinases from bovine heart

Dorothy E. Croall; George N. DeMartino

doi:10.1016/0167-4838(84)90048-7

Comparison of two calcium-dependent proteinases from bovine heart

Dorothy E. Croall, George N. DeMartino

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53 Scopus citations

Abstract

We have purified two calcium-dependent proteinases from bovine heart. Each enzyme was a heterodimer. One proteinase (designated CDP-I) contained subunits of 84 and 26 kDa. The other proteinase (designated CDP-II) contained subunits of 80 and 26 kDa. The large subunit of each proteinases accounted for the calciuim-dependent proteolytic activity of the respective enzyme and could be isolated from the small subunit by caseim-Sepharose affinity chromatography. The large subunits of CDP-I and CDP-II appeared to be distinctly different proteins, based on differences in peptide maps and on the lack of detectable immunologic cross-reactivity. On the other hand, the small subunits of the proteinase appeared to be identical peptides, based on peptide mapping and on two-dimensional gel electrophoresis. The function of the small subunit is unknown. The two calcium-dependent proteinases share many catalytic properties, including the nature of proteinase activity against several myofibrillar proteins. However, the proteinases were distinguished by different calcium-concentration requirements. CDP-II required 300 mgM Ca²⁺ for half-maximal activity and 750 mgM Ca²⁺ for full activity. CDP-I required only 30 mgM Ca²⁺ for half-maximal activity and 100 mgM for full activity.

Original language	English (US)
Pages (from-to)	348-355
Number of pages	8
Journal	Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
Volume	788
Issue number	3
DOIs	https://doi.org/10.1016/0167-4838(84)90048-7
State	Published - Aug 14 1984

Keywords

(Bovine heart)
Ca dependence
Protein degradation
Proteinase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology

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10.1016/0167-4838(84)90048-7

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title = "Comparison of two calcium-dependent proteinases from bovine heart",

abstract = "We have purified two calcium-dependent proteinases from bovine heart. Each enzyme was a heterodimer. One proteinase (designated CDP-I) contained subunits of 84 and 26 kDa. The other proteinase (designated CDP-II) contained subunits of 80 and 26 kDa. The large subunit of each proteinases accounted for the calciuim-dependent proteolytic activity of the respective enzyme and could be isolated from the small subunit by caseim-Sepharose affinity chromatography. The large subunits of CDP-I and CDP-II appeared to be distinctly different proteins, based on differences in peptide maps and on the lack of detectable immunologic cross-reactivity. On the other hand, the small subunits of the proteinase appeared to be identical peptides, based on peptide mapping and on two-dimensional gel electrophoresis. The function of the small subunit is unknown. The two calcium-dependent proteinases share many catalytic properties, including the nature of proteinase activity against several myofibrillar proteins. However, the proteinases were distinguished by different calcium-concentration requirements. CDP-II required 300 mgM Ca2+ for half-maximal activity and 750 mgM Ca2+ for full activity. CDP-I required only 30 mgM Ca2+ for half-maximal activity and 100 mgM for full activity.",

keywords = "(Bovine heart), Ca dependence, Protein degradation, Proteinase",

author = "Croall, {Dorothy E.} and DeMartino, {George N.}",

note = "Funding Information: This work was supported by grants from the National Institutes of Health (AM 29829 to GND) and the American Heart Association, Texas Affiliate (to DEC). We thank Julie Bower and Kelly Patrick for technical assistance and Mary Vaughn for preparation of the manuscript.",

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AU - Croall, Dorothy E.

AU - DeMartino, George N.

N1 - Funding Information: This work was supported by grants from the National Institutes of Health (AM 29829 to GND) and the American Heart Association, Texas Affiliate (to DEC). We thank Julie Bower and Kelly Patrick for technical assistance and Mary Vaughn for preparation of the manuscript.

PY - 1984/8/14

Y1 - 1984/8/14

N2 - We have purified two calcium-dependent proteinases from bovine heart. Each enzyme was a heterodimer. One proteinase (designated CDP-I) contained subunits of 84 and 26 kDa. The other proteinase (designated CDP-II) contained subunits of 80 and 26 kDa. The large subunit of each proteinases accounted for the calciuim-dependent proteolytic activity of the respective enzyme and could be isolated from the small subunit by caseim-Sepharose affinity chromatography. The large subunits of CDP-I and CDP-II appeared to be distinctly different proteins, based on differences in peptide maps and on the lack of detectable immunologic cross-reactivity. On the other hand, the small subunits of the proteinase appeared to be identical peptides, based on peptide mapping and on two-dimensional gel electrophoresis. The function of the small subunit is unknown. The two calcium-dependent proteinases share many catalytic properties, including the nature of proteinase activity against several myofibrillar proteins. However, the proteinases were distinguished by different calcium-concentration requirements. CDP-II required 300 mgM Ca2+ for half-maximal activity and 750 mgM Ca2+ for full activity. CDP-I required only 30 mgM Ca2+ for half-maximal activity and 100 mgM for full activity.

AB - We have purified two calcium-dependent proteinases from bovine heart. Each enzyme was a heterodimer. One proteinase (designated CDP-I) contained subunits of 84 and 26 kDa. The other proteinase (designated CDP-II) contained subunits of 80 and 26 kDa. The large subunit of each proteinases accounted for the calciuim-dependent proteolytic activity of the respective enzyme and could be isolated from the small subunit by caseim-Sepharose affinity chromatography. The large subunits of CDP-I and CDP-II appeared to be distinctly different proteins, based on differences in peptide maps and on the lack of detectable immunologic cross-reactivity. On the other hand, the small subunits of the proteinase appeared to be identical peptides, based on peptide mapping and on two-dimensional gel electrophoresis. The function of the small subunit is unknown. The two calcium-dependent proteinases share many catalytic properties, including the nature of proteinase activity against several myofibrillar proteins. However, the proteinases were distinguished by different calcium-concentration requirements. CDP-II required 300 mgM Ca2+ for half-maximal activity and 750 mgM Ca2+ for full activity. CDP-I required only 30 mgM Ca2+ for half-maximal activity and 100 mgM for full activity.

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KW - Proteinase

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Comparison of two calcium-dependent proteinases from bovine heart

Abstract

Keywords

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