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Spasmin and a Putative Spasmin Binding Protein(s) Isolated from Solubilized Spasmonemes 1
Author(s) -
Asai Hiroshi,
Ninomiya Takashi,
Kono RinIchiro,
Moriyama Yasushige
Publication year - 1998
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1998.tb05066.x
Subject(s) - calmodulin , biology , calcium , biochemistry , calcium binding protein , amino acid , methionine , tryptophan , amino acid residue , protein structure , solubilization , binding protein , peptide sequence , biophysics , enzyme , chemistry , gene , organic chemistry
The amino acid composition and hydrophobicity scale (hydropathy) of calcium‐binding proteins contained in the contractile spasmoneme of Carchesium polypinum was compared with other calcium‐binding proteins from eukaryotes. Spasmins which may hind at most 4 calcium ions simultaneously and initiate spasmoneme contraction cooperatively belong to a super family of proteins including; centrin/caltractin and calmodulin. Based on chemical modification of tryptophan and methionine, these residues are involved in contraction but the spasmin proteins contain little or none of these amino acids. Based on this evidence, it is suggested that another, non‐calcium binding protein(s) is involved in spasmoneme contraction.