FINE-STRUCTURE OF THE CHITIN PROTEIN SYSTEM IN THE CRAB CUTICLE
FINE-STRUCTURE OF THE CHITIN PROTEIN SYSTEM IN THE CRAB CUTICLE
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DOI:
10.1016/0040-8166(84)90020-x
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发表时间:
1984-01-01
期刊:
影响因子:
2.6
通讯作者:
GIRAUDGUILLE, MM
中科院分区:
文献类型:
--
作者:
GIRAUDGUILLE, MM
The fine structure of the organic matrix of the shore crab cuticle (C. maenas L.), observed in transmission electron microscopy, reveals 3 different levels of organization of the chitin-protein complex. The highest level corresponds to the twisted plywood organization described by Bouligand (1972). Horizontal microfibrils, parallel to the cuticle plane, rotate progressively from one level to another. When viewed in oblique section this structure gives superimposed series of nested arcs, visible in light microscopy or at the lowest magnifications of the EM, in all the chitin-protein layers. At the highest magnifications of the EM and with the best resolution, when the ultrathin sections are exactly transverse to the microfibril, a constant pattern can be observed which consists of rods transparent to electrons, which are embedded in an electron-opaque matrix. In cross-section, these rods often form more or less hexagonal arrays. A microfibril is one rod and the adjacent opaque material is another. The usual interpretation of the microfibril molecular structure is questioned. Between these 2 levels of organization, there is an intermediate level, which corresponds to the grouping of microfibrils. Microfibrils form a dense structure, with few free spaces in the membranous layer, the deepest and non-calcified layer of the cuticle. In other parts of the cuticle, microfibrils are grouped into fibrils of various diameters or form a reticulate structure, the free spaces of the organic matrix are occupied by the mineral.