Two low-molecular-weight Ca2+-binding proteins isolated from squid optic lobe by phenothiazine--Sepharose affinity chromatography.

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  • Author(s): Head JF; Spielberg S; Kaminer B
  • Source:
    The Biochemical journal [Biochem J] 1983 Mar 01; Vol. 209 (3), pp. 797-802.
  • Publication Type:
    Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Published by Portland Press on behalf of the Biochemical Society Country of Publication: England NLM ID: 2984726R Publication Model: Print Cited Medium: Print ISSN: 0264-6021 (Print) Linking ISSN: 02646021 NLM ISO Abbreviation: Biochem J Subsets: MEDLINE
    • Publication Information:
      Original Publication: London, UK : Published by Portland Press on behalf of the Biochemical Society
    • Subject Terms:
      Calcium-Binding Proteins/*isolation & purification ; Decapodiformes/*analysis ; Optic Lobe, Nonmammalian/*analysis; 3',5'-Cyclic-AMP Phosphodiesterases/metabolism ; Amino Acids/analysis ; Animals ; Calcium-Binding Proteins/pharmacology ; Calmodulin/isolation & purification ; Chlorpromazine/metabolism ; Chromatography, Affinity/methods ; Cyclic Nucleotide Phosphodiesterases, Type 1 ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation/drug effects ; Molecular Weight ; Phenothiazines ; Spectrophotometry, Ultraviolet
    • Abstract:
      We have isolated two Ca2+-binding proteins from squid optic lobes, each of which is also able to bind phenothiazines in a Ca2+-dependent manner. These proteins have each been purified and partly characterized. One of the proteins corresponds to calmodulin, in that it has a similar amino acid content to bovine brain calmodulin, including a single residue of trimethyl-lysine, it co-migrates with bovine calmodulin both on alkaline-urea- and on sodium dodecyl sulphate (SDS)/polyacrylamide-gel electrophoresis, and will activate calmodulin-dependent phosphodiesterase. The second protein has the same subunit molecular weight as calmodulin, as determined by SDS/polyacrylamide-gel electrophoresis, Mr 17 000, but migrates more slowly than this protein on alkaline-urea-gel electrophoresis. It has an amino acid composition distinct from calmodulin, containing no trimethyl-lysine, its CNBr fragments migrate on alkaline gels in a pattern distinct from those of calmodulin and it shows little ability to activate phosphodiesterase. The u.v.-absorption spectra of the proteins indicate the absence of tryptophan and the presence of a high phenylalanine/tyrosine ratio in each. Both proteins also bind 3-4 calcium ions/mol at 0.1 mM-free Ca2+ and each binds chlorpromazine in a Ca2+-dependent manner.
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    • Accession Number:
      0 (Amino Acids)
      0 (Calcium-Binding Proteins)
      0 (Calmodulin)
      0 (Phenothiazines)
      EC 3.1.4.17 (3',5'-Cyclic-AMP Phosphodiesterases)
      EC 3.1.4.17 (Cyclic Nucleotide Phosphodiesterases, Type 1)
      U42B7VYA4P (Chlorpromazine)
    • Publication Date:
      Date Created: 19830301 Date Completed: 19830811 Latest Revision: 20190501
    • Publication Date:
      20240829
    • Accession Number:
      PMC1154159
    • Accession Number:
      10.1042/bj2090797
    • Accession Number:
      6307266