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Isolation of a novel calcium‐binding protein from streptomyces erythreus
Author(s) -
Leadlay Peter F.,
Roberts Graham,
Walker John E.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81261-2
Subject(s) - calcium , calmodulin , biochemistry , calcium binding protein , binding protein , polyacrylamide gel electrophoresis , chemistry , binding site , gel electrophoresis , peptide sequence , dna binding protein , streptomyces , biology , bacteria , enzyme , genetics , gene , organic chemistry , transcription factor
A small, acidic protein has been isolated from Streptomyces erythreus . Like eukaryotic calcium‐binding proteins, it exhibits a calcium‐dependent shift in mobility on SDS‐polyacrylamide gel electrophoresis. Its N‐terminal amino acid sequence contains a potential calcium‐binding site which shows striking homology to the corresponding sites in calmodulin. Direct binding studies using 45 Ca showed that the protein, either purified or in cell‐free extracts, is capable of binding calcium with high affinity.