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Volumn 262, Issue 15, 1987, Pages 7429-7437
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Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sulfhydryl cross-linking. A mechanism for caldesmon's F-actin bundling activity.
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NONE
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Author keywords
[No Author keywords available]
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Indexed keywords
ACTIN;
CALMODULIN BINDING PROTEIN;
CALMODULIN BINDING PROTEINS;
CROSS LINKING REAGENT;
CROSS LINKING REAGENTS;
CYANOGEN BROMIDE;
CYSTEINE;
DISULFIDE;
PEPTIDE FRAGMENT;
THIOL DERIVATIVE;
ANIMAL;
ARTICLE;
AVIAN STOMACH;
CHICKEN;
METABOLISM;
MOLECULAR WEIGHT;
OXIDATION REDUCTION REACTION;
PROTEIN CONFORMATION;
RABBIT;
SMOOTH MUSCLE;
SOLUTION AND SOLUBILITY;
ACTINS;
ANIMAL;
CALMODULIN-BINDING PROTEINS;
CHICKENS;
CROSS-LINKING REAGENTS;
CYANOGEN BROMIDE;
CYSTEINE;
DISULFIDES;
GIZZARD;
MOLECULAR WEIGHT;
MUSCLE, SMOOTH;
OXIDATION-REDUCTION;
PEPTIDE FRAGMENTS;
PROTEIN CONFORMATION;
RABBITS;
SOLUTIONS;
SULFHYDRYL COMPOUNDS;
SUPPORT, U.S. GOV'T, P.H.S.;
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EID: 0023664509
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: None Document Type: Article |
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Times cited : (73)
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References (0)
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