Gibson G J, Francki K T, Hopwood J J, Foster B K
Department of Chemical Pathology, Adelaide Children's Hospital, South Australia.
Biochem J. 1991 Jul 15;277 ( Pt 2)(Pt 2):513-20. doi: 10.1042/bj2770513.
Direct comparison of type X collagen synthesized by human, sheep and chick growth-plate cartilage has shown that the human type X collagen is similar to the chick in both its molecular mass, containing component alpha-chains of 59 kDa with helical regions of 45 kDa, and apparent absence of disulphide-stabilized aggregates, whereas the sheep type X collagen has slightly larger alpha-chains (63 kDa) accounted for by a longer helical region (49 kDa) that contains cystine residues essential for the formation of the high-molecular-mass aggregates found with this species. Type X collagen from all three species showed heterogeneity in primary collagen structure as revealed by Staphylococcus aureus V8 proteinase-generated peptide maps. Collagen synthesis by growth-plate cartilage in culture, particularly synthesis of type IX and X collagen, was shown to be very sensitive to prior storage and suggests caution in the interpretation of changes detected when examining collagen synthesis by growth plates in culture.
对人、羊和鸡生长板软骨合成的X型胶原蛋白进行的直接比较表明，人X型胶原蛋白在分子量方面与鸡的相似，含有59 kDa的α链成分，其螺旋区域为45 kDa，且明显不存在二硫键稳定的聚集体；而羊X型胶原蛋白的α链略大（63 kDa），这是由更长的螺旋区域（49 kDa）导致的，该螺旋区域包含形成该物种中发现的高分子量聚集体所必需的胱氨酸残基。金黄色葡萄球菌V8蛋白酶生成的肽图谱显示，所有这三个物种的X型胶原蛋白在原胶原结构上均表现出异质性。培养的生长板软骨的胶原蛋白合成，尤其是IX型和X型胶原蛋白的合成，对先前的储存非常敏感，这表明在解释培养的生长板中胶原蛋白合成检测到的变化时应谨慎。
