In:
European Journal of Immunology, Wiley, Vol. 17, No. 11 ( 1987-01), p. 1625-1633
Abstract:
A novel proteinase, termed human T cell‐associated serine proteinase (HuTSP), has been highly purified from a human CD8 + T lymphocyte clone. By using a panel of chromogenic model peptide substrates the enzyme was found to specifically recognize L‐arginine and to cleave Tos‐Gly‐Pro‐Arg‐nitroanilide with high efficiency at a pH optimum of 10.5–11. Exposure to class‐specific proteinase inhibitors revealed that HuTSP is a serine endopeptidase. The enzyme has a mol. mass of ∼ 50 kDa (non‐reduced) and of ∼ 25–30 kDa (reduced) when analyzed by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis suggesting HuTSP to be a disulfide‐linked dimer. The enzyme is shown to be inducible by lectin in both CD4 + and CD8 + lymphocytes. Moreover, HuTSP was detected in a number of independent CD4 + and CD8 + T cell clones and was found to be released from effector cells upon ligand binding to the CD3‐T cell receptor complex.
Type of Medium:
Online Resource
ISSN:
0014-2980
,
1521-4141
DOI:
10.1002/eji.1830171116
Language:
English
Publisher:
Wiley
Publication Date:
1987
detail.hit.zdb_id:
1491907-2
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