The ear-shell (Sulculus diversicolor aquatilis) myoglobin is composed of an unusual 39 kDA polypeptide chain
- 1 October 1989
- journal article
- research article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 45 (10) , 998-1002
- https://doi.org/10.1007/bf01953061
Abstract
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.This publication has 18 references indexed in Scilit:
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