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|Title:||Expression of recombinant human Met-ase-1: a NK cell-specific granzyme.||Austin Authors:||Smyth, Mark J;O'Connor, M D;Kelly, J M;Ganesvaran, P;Thia, K Y;Trapani, Joseph A||Affiliation:||Cellular Cytotoxicity Laboratory, Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australia||Issue Date:||14-Dec-1995||Publication information:||Biochemical and Biophysical Research Communications; 217(2): 675-83||Abstract:||Human Met-ase-1 is a member of a family of cytotoxic lymphocyte serine proteases (granzymes), but is expressed specifically in CD3- large granular lymphocytes with natural killer cell activity. We have devised a polymerase chain reaction strategy to delete the predicted hexapropeptide of human Met-ase-1 (Ser-6 to Gln-1), to enable its expression and activation in mammalian COS cells. In addition, using peptide immunization we have derived a unique and specific monoclonal antibody detecting human Met-ase-1. Western blot analysis and protease assays of transfected COS cell lysates against a panel of thiobenzyl ester substrates formally demonstrated that the human Met-ase-1 gene encodes a serine proteinase that specifically hydrolyzes substrates containing a methionine (Met-) side chain at P1. The expression of active human Met-ase-1 and the generation of a specific anti-human Met-ase-1 monoclonal antibody will now enable a detailed structure/function analysis of key amino acids that confer this unusual serine protease specificity.||Gov't Doc #:||7503751||URI:||http://ahro.austin.org.au/austinjspui/handle/1/13016||URL:||https://pubmed.ncbi.nlm.nih.gov/7503751||Type:||Journal Article||Subjects:||Animals
Killer Cells, Natural.enzymology
Molecular Sequence Data
Protein Processing, Post-Translational
|Appears in Collections:||Journal articles|
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