Title : Primary structure of human
neutrophil elastase
Abstract :
- The complete amino acid sequence of human neutrophil elastase has been determined
- The protein consists of 218 amino acid residues , contains two asparagine-linked carbohydrate side chains, and is joined together by four disulfide bonds
- Comparison of the sequence to other serine proteinases indicates only moderate homology with porcine pancreatic elastase (43.0%) or neutrophil cathepsin G (37.2%)
- In particular, many of the residues suggested to play important roles in the mechanism by which the pancreatic elastase functions are significantly changed in the neutrophil enzyme , indicating alternative types of binding with the human proteinase
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. asparagine-linked, , -, two asparagine-linked carbohydrate side chains, asparagine
- 2. contains, , protein, two asparagine-linked carbohydrate side chains, -
Output(Part-Of) (sent_index,
protein,
site):
- 1. neutrophil elastase, sequence
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):