| Parvalbumins from coelacanth muscle. II. Amino acid sequence of the two less acidic components. | |
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MedLine Citation:
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PMID: 30486 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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J F Pechere; H Rochat; C Ferraz |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 536 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 1978 Sep |
Date Detail:
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Created Date: 1979-01-15 Completed Date: 1979-01-15 Revised Date: 2003-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 269-74 Citation Subset: IM |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Fishes Hydrogen-Ion Concentration Male Muscle Proteins* Muscles / analysis Parvalbumins* Peptide Fragments / analysis Trypsin |
| Chemical | |
Reg. No./Substance:
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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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