Structural changes induced by calcium and magnesium in a high affinity calcium-binding protein from crayfish sarcoplasm

The sarcoplasmic calcium-binding protein (SCP) from crayfish has in its dimer form two calcium-specific and four Ca-Mg sites. The conformations of this protein in the calcium- (SCP sub(2) multiplied by Ca sub(6)), magnesium- (SCP sub(2) multiplied by Mg sub(4)), and metal-free forms as well as in in...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 256; no. 22; pp. 11538 - 11544
Main Authors Wnuk, W, Cox, J A, Stein, E A
Format Journal Article
LanguageEnglish
Published United States 25.11.1981
Subjects
Animals
Astacoidea
Astacura
Binding Sites
C.D
calcium
Calcium - pharmacology
calcium-binding protein
Calcium-Binding Proteins - metabolism
chemical properties
Circular Dichroism
fluorescence
Freshwater
Kinetics
Macromolecular Substances
magnesium
Magnesium - pharmacology
Protein Conformation
proteins
sarcoplasmic reticulum
Sarcoplasmic Reticulum - metabolism
Spectrometry, Fluorescence
Trypsin
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Summary:The sarcoplasmic calcium-binding protein (SCP) from crayfish has in its dimer form two calcium-specific and four Ca-Mg sites. The conformations of this protein in the calcium- (SCP sub(2) multiplied by Ca sub(6)), magnesium- (SCP sub(2) multiplied by Mg sub(4)), and metal-free forms as well as in intermediary states have been studied by circular dichroism (CD) in the far and near-ultraviolet regions, tryptophan fluorescence, sulfhydryl reactivity, and trypsin susceptibility.
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ISSN:0021-9258
DOI:10.1016/S0021-9258(19)68434-6