Autodegradation of 125I-labeled human epidermal cell surface proteins.

Journal Article (Journal Article)

Triton X-100 extracts of cultured human epidermal cells exhibited proteolytic activity as measured by the hydrolysis of [3H]-casein at neutral pH. The majority of endogenous proteolytic activity was inhibited by parahydroxy mercuribenzoate and by mersalyl acid, indicating the enzyme(s) was a thiol class proteinase(s). Crude Triton X-100 extracts were prepared from epidermal cells following labeling of proteins with 125I. Autodegradation of labeled proteins at 37 degrees C was detected as early as 1 hr and reached a plateau level by 4 hr. Degradation was inhibited by thiol class proteinase inhibitors. Among the detergent-solubilized radiolabeled proteins a polypeptide chain of Mr 155,000 was particularly sensitive to degradation by endogenous thiol proteinase(s).

Full Text

Duke Authors

Cited Authors

  • Hashimoto, K; Singer, KH; Lazarus, GS

Published Date

  • December 1, 1982

Published In

Volume / Issue

  • 79 / 6

Start / End Page

  • 361 - 364

PubMed ID

  • 6754823

International Standard Serial Number (ISSN)

  • 0022-202X

Digital Object Identifier (DOI)

  • 10.1111/1523-1747.ep12529445


  • eng

Conference Location

  • United States