牦牛皮胶原蛋白的提取及其性能分析

以牦牛皮为原料,提取了酸溶性胶原蛋白(ASC)和酶溶性胶原蛋白(PSC),并对胶原蛋白分子的结构和性能进行了分析。结果表明:ASC和PSC的提取率分别为54%±0.18%和78%±0.42%;UV、FTIR及电泳分析结果表明:ASC和PSC具有完整的三股螺旋结构,符合Ⅰ型胶原蛋白的结构特征;氨基酸分析发现:ASC和PSC含有丰富的亚氨基酸,其含量分别为264.1和276.6残基/1000残基;热稳定性分析表明:ASC和PSC热变性温度(Td)分别为37.5、41.5℃,热收缩温度分别为62.5、70.0℃,证明PSC的热稳定性高于ASC;SEM结果表明:ASC和PSC表面为松散、不规则的纤维网形态;自组装实验结果显示:两者具有一定的成纤维能力,自组装产物的D-周期分别为(68.2±5)nm、(69.3±3)nm,且PSC比ASC的组装速度快。     

An X-ray diffraction analysis of rat tail tendons treated with Cupromeronic Blue

Cupromeronic Blue was used to stain selectively the proteoglycans in rat tail tendons under ‘critical electrolyte’ conditions. Earlier electron microscopical observations indicated that at least one type of proteoglycan filament is associated with tendon collagen fibrils at the positive staining band ‘d’. To ensure that this was not an artefact caused by specimen preparation or the subsequent positive staining of the collagen fibrils, we have analysed low angle meridional diffraction patterns from stained but not dehydrated, embedded or counterstained tissues. Axial electron density profiles of Cupromeronic Blue-stained compared with unstained rat tail tendons revealed the axial locations and relative amounts of dye in both mature and young wet specimens. In mature tendons, the difference electron density profile contained a broad peak centred near residue 180 along the 234-residue D-period. This corresponds to the electron-optical staining band ‘d’. In young tendons a similar distribution of stain was observed although in this case there was evidence of a doublet of peaks, one centred near residue 182 (band ‘d’) and the other near residue 165 (midway between bands d and e₁). The wet proteoglycan-Cupromeronic Blue complexes distribute over about 30 nm along the collagen fibril axis. Comparison with the images of filaments seen in the electron microscope suggests that the dye complexes collapse significantly on dehydration and embedding.     

An AFM study of the nanostructural response of New Zealand white rabbit Achilles tendons to cyclic loading

The nanostructural response of New Zealand white rabbit Achilles tendons to a fatigue damage model was assessed quantitatively and qualitatively using the endpoint of dose assessments of each tendon from our previous study. The change in mechanical properties was assessed concurrently with nanostructural change in the same non-viable intact tendon. Atomic force microscopy was used to study the elongation of D-periodicities, and the changes were compared both within the same fibril bundle and between fibril bundles. D-periodicities increased due to both increased strain and increasing numbers of fatigue cycles. Although no significant difference in D-periodicity lengthening was found between fibril bundles, the lengthening of D-periodicity correlated strongly with the overall tendon mechanical changes. The accurate quantification of fibril elongation in response to macroscopic applied strain assisted in assessing the complex structure–function relationship in Achilles tendons.