Purification and properties of caldesmon-like protein from molluscan smooth muscle

A. Málnási-Csizmadia, Armelle Bonet-Kerrache, L. Nyitray, Dominique Mornet

Research output: Article

16 Citations (Scopus)

Abstract

In this comparative study, the heat-stable protein content of scallop muscles was reinvestigated. The hCaD-like protein was prepared and its properties carefully examined. The heat-stable high-molecular-mass caldesmon-like (hCaD-like) protein is only present in the catch (smooth) muscle and it is completely absent in the striated muscle of scallop. The isolated scallop hCaD-like protein cosediments with F-actin, binds to myosin significantly and inhibits the ATPase activity of acto-myosin. A partial cDNA clone from a Mytilus anterior byssus retractor muscle (ABRM)-related protein showed strong homology with the hCaD gizzard sequence. This allowed identification of the heat-stable 100-110 kDa protein doublet band isolated in this study as a caldesmon-like molecule.

Original languageEnglish
Pages (from-to)59-63
Number of pages5
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume108
Issue number1
DOIs
Publication statusPublished - 1994

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Calmodulin-Binding Proteins
Purification
Smooth Muscle
Muscle
Pectinidae
Molecular mass
Hot Temperature
pioglitazone
Myosins
Proteins
Mytilus
Striated Muscle
Muscle Proteins
Adenosine Triphosphatases
Actins
Complementary DNA
Clone Cells
Muscles
Molecules

Cite this

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abstract = "In this comparative study, the heat-stable protein content of scallop muscles was reinvestigated. The hCaD-like protein was prepared and its properties carefully examined. The heat-stable high-molecular-mass caldesmon-like (hCaD-like) protein is only present in the catch (smooth) muscle and it is completely absent in the striated muscle of scallop. The isolated scallop hCaD-like protein cosediments with F-actin, binds to myosin significantly and inhibits the ATPase activity of acto-myosin. A partial cDNA clone from a Mytilus anterior byssus retractor muscle (ABRM)-related protein showed strong homology with the hCaD gizzard sequence. This allowed identification of the heat-stable 100-110 kDa protein doublet band isolated in this study as a caldesmon-like molecule.",
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T1 - Purification and properties of caldesmon-like protein from molluscan smooth muscle

AU - Málnási-Csizmadia, A.

AU - Bonet-Kerrache, Armelle

AU - Nyitray, L.

AU - Mornet, Dominique

PY - 1994

Y1 - 1994

N2 - In this comparative study, the heat-stable protein content of scallop muscles was reinvestigated. The hCaD-like protein was prepared and its properties carefully examined. The heat-stable high-molecular-mass caldesmon-like (hCaD-like) protein is only present in the catch (smooth) muscle and it is completely absent in the striated muscle of scallop. The isolated scallop hCaD-like protein cosediments with F-actin, binds to myosin significantly and inhibits the ATPase activity of acto-myosin. A partial cDNA clone from a Mytilus anterior byssus retractor muscle (ABRM)-related protein showed strong homology with the hCaD gizzard sequence. This allowed identification of the heat-stable 100-110 kDa protein doublet band isolated in this study as a caldesmon-like molecule.

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