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.
|Number of pages||6|
|Journal||European Journal of Biochemistry|
|Publication status||Published - 1987 Aug|