Scott P G, Veis A
Connect Tissue Res. 1976;4(2):107-16. doi: 10.3109/03008207609152206.
Acid soluble collagen and purified alpha1 and alpha2 chains were prepared from bovine skin and digested with cyanogen bromide. The resultant peptides were separated by electrophoresis on polyacrylamide gels containing sodium dodecylsulphate. Thirteen peptides obtained from the alpha1 chain and two from the alpha2 chain were identified as overlapping sequences containing methionine-derived peptide bonds not cleaved during the reaction. Those uncleaved peptides from the alpha1 chain accounted for approximately 30% of the total digest, as determined by planimetry on the staining profiles, and their relative proportions indicated that efficiency of cleavage at specific methionine residues was dependent upon position in the sequence. Alpha1CB5-8 was most resistant to cleavage while alpha1CB0,1-2 and alpha1CB7-6 were most susceptible. Peptides of a 2:1 (w/w) mixture of alpha1 and alpha2 chains and of the acid-soluble collagen gave electrophoretograms which were essentially a summation of those obtained from the individual chains.
从牛皮中制备酸溶性胶原蛋白以及纯化的α1和α2链，并用溴化氰进行消化。所得肽段通过在含有十二烷基硫酸钠的聚丙烯酰胺凝胶上进行电泳分离。从α1链获得的13个肽段和从α2链获得的2个肽段被鉴定为含有在反应过程中未被切割的甲硫氨酸衍生肽键的重叠序列。通过对染色图谱进行平面测量确定，来自α1链的那些未切割肽段约占总消化物的30%，并且它们的相对比例表明，在特定甲硫氨酸残基处的切割效率取决于序列中的位置。α1CB5 - 8对切割最具抗性，而α1CB0,1 - 2和α1CB7 - 6最易被切割。α1和α2链以及酸溶性胶原蛋白的2:1（w/w）混合物的肽段给出的电泳图谱基本上是从各个链获得的图谱的总和。
