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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