Calcified Tissue Research

, Volume 25, Issue 1, pp 45–51 | Cite as

The crystal sheaths from bivalve hinge ligaments

  • Mary Marsh
  • Gary Hamilton
  • Ronald Sass
Article
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Revised:
Accepted:

Summary

The aragonite crystals in the molluscan bivalve hinge ligament are surrounded by an organic sheath which is distinct from the remainder of the ligament matrix.

Methods have been developed to isolate these sheathed crystals from the ligaments ofSpisula solidissima andMercenaria mercenaria employing a papain digestion of the matrix protein. The sheathed crystals fromSpisula have a CaCO3/protein ratio of 11.1 and those fromMercenaria a ratio of 29.6. The sheathed crystals and the empty crystal sheaths have been examined by electron microscopy for structural integrity.

The sheath proteins exhibit much smaller proportions of the amino acids glycine and methionine than the hinge ligaments. These are characteristic amino acids of high concentration in the hinge ligaments of both species. The concentrations of acidic and basic amino acids are increased about two fold in the sheaths over those of the ligaments. Otherwise there is little similarity in the amino acid composition of the sheaths in the two species. However, SDS electrophoresis shows the sheaths of both to contain a major protein component with a molecular weight of about 25,000. The sheath protein from theMercenaria ligament contains about 5% carbohydrate and that ofSpisula sheaths less than 1% carbohydrate.

Key words

CaCO3 Amino acids Sheaths Ligament Electron microscopy 
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Copyright information

© Springer-Verlag 1978

Authors and Affiliations

  • Mary Marsh
    • 1
  • Gary Hamilton
    • 1
  • Ronald Sass
    • 1
  1. 1.Department of Chemistry and Department of BiologyRice UniversityHoustonUSA

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