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. 1969 Jun;113(1):39–47. doi: 10.1042/bj1130039

Subunit structure of oyster paramyosin

E F Woods 1
PMCID: PMC1184602  PMID: 5806395

Abstract

Paramyosin from the oyster Crassostrea commercialis was studied by equilibrium sedimentation. In non-denaturing solvents the minimum molecular weight is 208000. Dissociation into subunits requires complete disruption of the α-helix. This occurs at pH7 in guanidine hydrochloride solutions of concentration greater than 7m in the presence of a disulphide-bond-reducing agent. Solutions of the protein in concentrated guanidine hydrochloride are polydisperse and contain species of low molecular weight (approx. 25000) comprising approx. 5% to 10% of the protein. The molecular weight of the main component is estimated to be 97000 and the paramyosin molecule contains two of these subunits. From the present observations no decision can be made as to whether or not the small component (or components) represents part of the paramyosin molecule. Preferential binding of guanidine hydrochloride to the extent of 0·13g./g. of protein was shown in solutions of paramyosin in 7·85m-guanidine hydrochloride.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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