Document Detail


Amino acid sequence of calmodulin from Euglena gracilis.
MedLine Citation:
PMID:  1572365     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The complete amino acid sequence of calmodulin from Euglena gracilis was determined by isolation and sequence analyses of peptides derived from calmodulin by digestion with trypsin and Staphylococcus aureus V8 protease. Euglena calmodulin consists of 148 amino acid residues; it lacks tryptophan and cysteine and contains one tyrosine, three histidine and two NE-trimethyllysine residues/molecule of the protein. Its N-terminus was blocked with an acetyl group and C-terminal lysine was trimethylated. Euglena calmodulin is the first calmodulin so far examined in which the C-terminal lysine is trimethylated. The comparison of amino acid sequences between Euglena and human brain calmodulins indicated 17 amino acid substitutions in Euglena calmodulin.
Authors:
H Toda; M Yazawa; K Yagi
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  205     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1992 Apr 
Date Detail:
Created Date:  1992-06-02     Completed Date:  1992-06-02     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  653-60     Citation Subset:  IM    
Affiliation:
Institute for Protein Research, Osaka University, Japan.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/P11118
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Calmodulin / chemistry*,  genetics,  isolation & purification
Chromatography, High Pressure Liquid
Euglena gracilis / genetics,  metabolism*
Humans
Molecular Sequence Data
Peptide Fragments / isolation & purification
Sequence Homology, Nucleic Acid
Serine Endopeptidases
Trypsin
Chemical
Reg. No./Substance:
0/Calmodulin; 0/Peptide Fragments; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.19/glutamyl endopeptidase; EC 3.4.21.4/Trypsin

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