NEUTRON-DIFFRACTION STUDIES OF COLLAGEN IN FULLY MINERALIZED BONE

NEUTRON-DIFFRACTION STUDIES OF COLLAGEN IN FULLY MINERALIZED BONE
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DOI:
10.1016/0022-2836(85)90090-7
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发表时间:
1985-01-01
影响因子:
5.6
通讯作者:
MOOK, HA
MOOK, HA
中科院分区:
生物学2区
文献类型:
--
作者:
BONAR, LC;LEES, S;MOOK, HA

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在潮湿和干燥条件下,对完全矿化的成熟牛骨和去矿化骨胶原中的胶原蛋白的赤道和经向间距进行了中子衍射测量。湿矿化牛骨中的胶原赤道间距为1.24 nm,显着低于在湿脱矿牛骨胶原中观察到的1.53 nm值。干骨和脱矿骨胶原的相应间距分别为 1.16 nm 和 1.12 nm。矿化牛骨中胶原蛋白经向长间距为63.6 nm湿态和63.4 nm干态。完全矿化的牛骨中的胶原蛋白可能比之前假设的更加紧密地堆积,其堆积密度类似于相对结晶的胶原蛋白(例如湿鼠尾腱)的堆积密度。显然,牛骨中胶原纤维内可供矿物质使用的空间比之前假设的要少。骨头中矿物质的主要部分必须位于原纤维之外。
Neutron diffraction measurements have been made of the equatorial and meridional spacings of collagen in fully mineralized mature bovine bone and dimineralized bone collagen, in both wet and dry conditions. The collagen equatorial spacing in wet mineralized bovine bone is 1.24 nm, substantially lower than the 1.53 nm value observed in wet demineralized bovine bone collagen. Corresponding spacings for dry bone and demineralized bone collagen are 1.16 nm and 1.12 nm, respectively. The collagen meridional long spacing in mineralized bovine bone is 63.6 nm wet and 63.4 nm dry. Collagen in fully mineralized bovine bone may be considerably more closely packed than had been assumed previously, with a packing density similar to that of the relatively crystalline collagens such as wet rat tail tendon. Apparently, less space is available for mineral within the collagen fibrils in bovine bone than had previously been assumed; the major portion of the mineral in this bone must be located outside the fibrils.