Glanville R W, Rauter A
Hoppe Seylers Z Physiol Chem. 1981 Jul;362(7):943-51. doi: 10.1515/bchm2.1981.362.2.943.
The pepsin digestion of human placental type IV collagen was studied in order to gain insight into the relationships between the fragments alpha 1(IV)95 000 and alpha 2(IV)70 000 which have previously been described. (For nomenclature see Crouch, E., Sage, H. & Bornstein, P. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 745-749.) Seven smaller pepsin fragments with apparent molecular weights in the range of Mr = 5 000 to 50 000 were also isolated and characterized. The amino-terminal amino acid sequences of alpha 1 (IV)95 000, alpha 2(IV) 70 000 and the smaller pepsin fragments are presented. Kinetic data on the pepsin solubilization provided evidence for the presence of at least two different collagen triple helices within basement membranes and sequence data demonstrated the presence of a number of short non-collagen-like sequences which interrupt the triple helical regions of the alpha chains.
为了深入了解先前已描述的α1(IV)95000和α2(IV)70000片段之间的关系,对人胎盘IV型胶原的胃蛋白酶消化进行了研究。(命名法见Crouch, E., Sage, H. & Bornstein, P. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 745 - 749。)还分离并鉴定了七个表观分子量在Mr = 5000至50000范围内的较小胃蛋白酶片段。给出了α1(IV)95000、α2(IV)70000和较小胃蛋白酶片段的氨基末端氨基酸序列。胃蛋白酶溶解的动力学数据为基底膜中至少存在两种不同的胶原三螺旋提供了证据,序列数据表明存在许多中断α链三螺旋区域的短非胶原样序列。