Wada K, Takai T, Tanabe T
Eur J Biochem. 1987 Aug 17;167(1):13-8. doi: 10.1111/j.1432-1033.1987.tb13298.x.
The complete amino acid sequences of the heavy and light chains of chicken liver cathepsin L have been determined by automated gas-phase Edman degradation. The heavy and light chains contained 176 and 42 amino acid residues respectively. A glucosamine-based oligosaccharide group was attached to Asn-109 of the heavy chain. Chicken liver cathepsin L had high sequence homology with rat cathepsin H, but exhibited less similarity with rat cathepsin B. Comparisons of cathepsin L with plant cysteine proteinases, such as papain, actinidin and aleurain, reveal high degree of homology.
鸡肝组织中组织蛋白酶L重链和轻链的完整氨基酸序列已通过自动气相Edman降解法测定。重链和轻链分别包含176个和42个氨基酸残基。一个基于氨基葡萄糖的寡糖基团连接在重链的Asn-109处。鸡肝组织蛋白酶L与大鼠组织蛋白酶H具有高度的序列同源性,但与大鼠组织蛋白酶B的相似性较低。组织蛋白酶L与植物半胱氨酸蛋白酶(如木瓜蛋白酶、猕猴桃蛋白酶和黑曲霉蛋白酶)的比较显示出高度的同源性。