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  • Life and Medical Sciences  (2)
  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 189 (1986), S. 261-270 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Three regions of the byssus of the marine mussel Mytilus edulis L. are distinct in structural organization at the macroscopic and microscopic level and in amino acid composition. The threads that emanate from the stem at the base of the foot are divided into two regions. The proximal, elastic region has a crimped, densely staining cortex enclosing an interior matrix of spiral fibers, and its amino acid composition reflects protein heterogeneity. The more distal, rigid region has a straight, tubular cortex surrounding an inner matrix of linearly arranged bundles of fibrils and has a composition approximating pure collagen. The plaque, or disc-shaped portion, which mediates attachment to various substrates, is distinguished by a surface matrix of collagen-like fibers similar to those of the thread region and anchored on an inner spongy matrix. Compositional evidence exists for a collagenous component, a catechol-rich protein, and at least one other accessory protein in the plaque.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Journal of Morphology 189 (1986), S. 171-181 
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The acellular attachment organ (byssus) of the marine mussel Mytilus edulis L. is composed of threads that emanate from the body of the mussel to adhesive discs that anchor the threads to rocks, sand and other mussels. Three proteins have been purified by immunohistological methods and located to specific regions of the byssus. A collagenous protein with subunit molecular weights of 53,000, 55,000 and 65,000 is found in the matrix of the elastic thread region. Its 73,000-MW precursor was extracted from foot glands in the area proximal to the animal body and was identified by immune cross-reactivity. A cystine-rich, acidic protein was found in all regions of the byssus associated with a third protein, the polyphenolic protein. The L-dopa-containing polyphenolic protein appears in the cortex of the entire thread and adhesive plaque and at the substrate-plaque interface. Antiserum to this protein stains spherical vesicles in the phenol gland of the foot. Using immuno-electrophoretic methods, the polyphenolic protein and the cystine-rich protein were shown to form high molecular weight aggregates with aging of the byssus.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
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