Document Detail


Parvalbumins from coelacanth muscle. II. Amino acid sequence of the two less acidic components.
MedLine Citation:
PMID:  30486     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The primary structure of the two less acidic parvalbumins (pI = 5.44 and pI = 4.95) from coelacanth muscle (Latimeria chalumnae) has been determined. They differ only by the presence or absence of a N-terminal blocking group. By the use of the automatic degradation, 69 amino acids could be placed unambiguously in the N-terminal part and 24 amino acids following the single arginine 75. Tryptic peptides were used to establish the sequence and the position of the remaining residues. The two parvalbumins examined belong to the alpha-lineage, and the rate of their molecular evolution is comparable to that found in other vertebrates.
Authors:
J F Pechere; H Rochat; C Ferraz
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  536     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1978 Sep 
Date Detail:
Created Date:  1979-01-15     Completed Date:  1979-01-15     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  269-74     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Fishes
Hydrogen-Ion Concentration
Male
Muscle Proteins*
Muscles / analysis
Parvalbumins*
Peptide Fragments / analysis
Trypsin
Chemical
Reg. No./Substance:
0/Muscle Proteins; 0/Parvalbumins; 0/Peptide Fragments; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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