The ear-shell (Sulculus diversicolor aquatilis) myoglobin is composed of an unusual 39 kDA polypeptide chain.
An unusual myoglobin was isolated from the buccal mass of the ear-shell Sulculus diversicolor aquatilis. The myoglobin consists of a 39 kDa polypeptide chain which is about double the size of the usual myoglobin subunit, contains one heme per molecule, and has an unusual spectral property ion the oxy-form. On the basis of these properties and partial amino acid sequencing, we propose that Sulculus myoglobin has a didomain structure, and that one of the two domains does not function as an oxygen-binding domain. So far, a myoglobin of this type has not been described in molluscs.
Suzuki
T
T
Department of Biology, Kochi University, Japan.
Furukohri
T
T
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006418:Heme / Q000032:analysis; D007700:Kinetics; D008969:Molecular Sequence Data; D008974:Mollusca / Q000032:analysis*; D009211:Myoglobin / Q000302:isolation & purification*; D010084:Oxidation-Reduction
D000596:Amino Acids; D009211:Myoglobin; D006418:Heme