Osteogenesis imperfecta: biochemical studies of bone collagen.
Osteogenesis imperfecta: biochemical studies of bone collagen.
复制标题
成骨不全：骨胶原的生化研究。
DOI：
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发表时间：
1977
影响因子：
4.2
通讯作者：
M. Tanzer
中科院分区：
文献类型：
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作者：
K. Fujii;M. Tanzer
从成骨迟缓症患者胫骨中提取胶原蛋白，通过氨基酸组成、亚基组成和交联形成研究其生化性质。将该骨骼与正常骨骼进行直接比较，年龄和性别匹配，这些骨骼在意外死亡后48小时内从个体的胫骨中取出。OI和正常骨胶原的氨基酸组成几乎相同，胃蛋白酶溶解的胶原组分以及不溶性骨胶原的CNBr肽非常相似，表明OI与正常骨胶原相比，胶原基因类型没有差异。NaB3H4还原后测定不溶性胶原的交联含量和比放射性。发现OI骨胶原的比放射性值平均比正常胶原高50%。OI胶原蛋白的分析表明，丰富的主要可还原醛和交联的形成。与对照组相比，还原的醛、二羟基正亮氨酸和还原的交联、二羟基赖氨酸正亮氨酸的比例高得多。这些结果可能表明OI骨胶原交联成熟延迟，并可能反映骨发育期间此类胶原稳定性降低。
The biochemical properties of tibial bone collagen, obtained from patients with osteogenesis imperfecta, were studied by investigating amino acid composition, subunit composition and crosslink formation. Direct comparison of this bone was made with normal bone, age and sex matched, which had been removed from the tibiae of individuals within 48 hours after accidental death. The amino acid compositions of OI and normal bone collagen were almost identical and the pepsin solubilized collagen fraction as well as the CNBr peptides of insoluble bone collagen were very similar, indicating that no differences in collagen genetic type occurred in OI compared to normal. The crosslink contents and the specific radioactivities of the insoluble collagens were determined following NaB3H4 reduction. The specific radioactivity values of OI bone collagen were found to average 50 per cent higher than normal collagen. Analyses of OI collagen showed abundant formation of the major reducible aldehydes and crosslinks. Compared to the controls there were much higher proportions of the reduced aldehyde, dihydroxynorleucine and the reduced crosslink, dihydroxylysinonorleucine. These results may indicate delayed maturation of crosslinking in OI bone collagen and may reflect diminished stability of such collagen during bone development.