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  • 11
    Electronic Resource
    Electronic Resource
    The ear-shell (Sulculus diversicolor aquatilis) myoglobin is composed of an unusual 39 kDA polypeptide chain (1989)
    Springer
    Cellular and molecular life sciences 45 (1989), S. 998-1002 
    Details
    ISSN: 1420-9071
    Keywords: Myoglobin ; didomain structure ; Sulculus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary An unusual myoglobin was isolated from the buccal mass of the ear-shellSulculus 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 in the oxy-form. On the basis of these properties and partial amino acid sequencing, we propose thatSulculus 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 mollusos.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01953061
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