Purification and characterization of the heat-stable calmodulin-binding protein from the matrix of bovine heart mitochondria

Osamu Hatase; Masaaki Tokuda; Rajendra K. Sharma; Jerry H. Wang; David E. Green

doi:10.1016/0006-291X(83)91773-4

Purification and characterization of the heat-stable calmodulin-binding protein from the matrix of bovine heart mitochondria

Osamu Hatase^*
, Masaaki Tokuda
, Rajendra K. Sharma
, Jerry H. Wang
, David E. Green

^*Corresponding author for this work

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

13 Citations (Scopus)

Abstract

A heat-stable calmodulin binding protein was purified and characterized from the matrix of bovine heart mitochondria. It bound specifically to calmodulin in the presence of calcium, and strongly inhibited the stimulatory activity of calmodulin on phosphodiesterase. The estimated molecular weight of the calmodulin-binding protein was 61,000 dalton determined by SDS-polyacrylamide gel electrophoresis.

Original language	English
Pages (from-to)	633-637
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	113
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(83)91773-4
Publication status	Published - 15 Jun 1983
Externally published	Yes

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10.1016/0006-291X(83)91773-4

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title = "Purification and characterization of the heat-stable calmodulin-binding protein from the matrix of bovine heart mitochondria",

abstract = "A heat-stable calmodulin binding protein was purified and characterized from the matrix of bovine heart mitochondria. It bound specifically to calmodulin in the presence of calcium, and strongly inhibited the stimulatory activity of calmodulin on phosphodiesterase. The estimated molecular weight of the calmodulin-binding protein was 61,000 dalton determined by SDS-polyacrylamide gel electrophoresis.",

author = "Osamu Hatase and Masaaki Tokuda and Sharma, \{Rajendra K.\} and Wang, \{Jerry H.\} and Green, \{David E.\}",

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T1 - Purification and characterization of the heat-stable calmodulin-binding protein from the matrix of bovine heart mitochondria

AU - Hatase, Osamu

AU - Tokuda, Masaaki

AU - Sharma, Rajendra K.

AU - Wang, Jerry H.

AU - Green, David E.

PY - 1983/6/15

Y1 - 1983/6/15

N2 - A heat-stable calmodulin binding protein was purified and characterized from the matrix of bovine heart mitochondria. It bound specifically to calmodulin in the presence of calcium, and strongly inhibited the stimulatory activity of calmodulin on phosphodiesterase. The estimated molecular weight of the calmodulin-binding protein was 61,000 dalton determined by SDS-polyacrylamide gel electrophoresis.

AB - A heat-stable calmodulin binding protein was purified and characterized from the matrix of bovine heart mitochondria. It bound specifically to calmodulin in the presence of calcium, and strongly inhibited the stimulatory activity of calmodulin on phosphodiesterase. The estimated molecular weight of the calmodulin-binding protein was 61,000 dalton determined by SDS-polyacrylamide gel electrophoresis.

UR - https://openalex.org/W1987321488

UR - https://www.webofscience.com/wos/woscc/full-record/WOS:A1983QU89200038

UR - https://www.scopus.com/pages/publications/0020960799

U2 - 10.1016/0006-291X(83)91773-4

DO - 10.1016/0006-291X(83)91773-4

M3 - Journal Article

C2 - 6870876

AN - SCOPUS:0020960799

SN - 0006-291X

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SP - 633

EP - 637

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Purification and characterization of the heat-stable calmodulin-binding protein from the matrix of bovine heart mitochondria

Abstract

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