Rigo Cristina, Bairati Aurelio
Dipartimento di Fisiologia e Biochimica Generali, Sezione di Istologia ed Anatomia Umana, Università degli Studi di Milano, via Celoria 26, 20133 Milan, Italy.
Cell Tissue Res. 2002 Nov;310(2):253-6. doi: 10.1007/s00441-002-0619-7. Epub 2002 Aug 21.
Guanidinium chloride treatment of Sepia officinalis cartilage solubilized a component that contained hydroxyproline. Electron-microscopy observation of rotary-shadowed preparations of this component revealed it to consist of rod-like units themselves consisting of filaments. Dialysis of an acetic acid solution against ATP afforded polymeric aggregates consisting of a succession of two or three thick sections showing transverse electron-opaque banding, separated by thinner sections without banding. Electrophoresis produced a main band of about 140 kDa sensitive to bacterial collagenase. After reduction with mercaptoethanol, electrophoresis afforded a 40-kDa band. Pepsin digestion resulted in additional electrophoretic bands. These data suggest the presence of a collagen in Sepia cartilage with characteristics unlike those of any known collagen.
用氯化胍处理乌贼软骨可溶解一种含羟脯氨酸的成分。对该成分旋转阴影制备物进行电子显微镜观察发现，它由杆状单元组成，而这些杆状单元本身又由细丝构成。用醋酸溶液对ATP进行透析可得到聚合物聚集体，该聚集体由两到三个连续的厚节段组成，厚节段呈现横向电子不透明条纹，中间由无条纹的较薄节段隔开。电泳产生一条约140 kDa的主带，该主带对细菌胶原酶敏感。用巯基乙醇还原后，电泳得到一条40 kDa的带。胃蛋白酶消化产生了额外的电泳条带。这些数据表明乌贼软骨中存在一种胶原蛋白，其特性与任何已知胶原蛋白都不同。
