A cytotoxic proteinase isolated from human lymphocytes.

Journal Article (Journal Article)

A proteinase active at physiologic pH was isolated from unstimulated human peripheral blood lymphocytes with gel filtration and affinity chromatography. The proteinase with a molecular mass of approximately 30,000 daltons was completely inhibited by diisopropylfluorophosphate (DFP) and soybean trypsin inhibitor (STI). Incubation of the lymphocyte enzyme with 3H-proline labeled T24 human bladder carcinoma cells resulted in significant cytoxicity of the target cells. Cytotoxicity was only observed with much higher concentrations of trypsin. Similar results were obtained with a 51Cr release assay. This investigation demonstrates that unstimulated human peripheral blood lymphocytes contain a cytotoxic proteinase capable of killing pre-labeled target cells. The proteinase may be involved in lymphocyte-mediated cytotoxicity.

Full Text

Duke Authors

Cited Authors

  • Hatcher, VB; Oberman, MS; Lazarus, GS; Grayzel, AI

Published Date

  • February 1, 1978

Published In

Volume / Issue

  • 120 / 2

Start / End Page

  • 665 - 670

PubMed ID

  • 621401

International Standard Serial Number (ISSN)

  • 0022-1767


  • eng

Conference Location

  • United States