| Literature DB >> 3305012 |
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.Entities:
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Year: 1987 PMID: 3305012 DOI: 10.1111/j.1432-1033.1987.tb13298.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956