Abstract
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.
Original language | English |
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Pages (from-to) | 13-18 |
Number of pages | 6 |
Journal | European Journal of Biochemistry |
Volume | 167 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1987 Aug |
Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry