Isolation and immunological characterization of the mammalian 32- 34-kDa stress protein

Madelyn M. Caltabiano, George Poste, Russell G. Greig

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Challenge of mammalian cells with heavy metals or sulfhydryl-reactive agents including sodium arsenite induces the de novo synthesis of a 32- 34-kDa stress protein (p32) (M. M. Caltabiano, T. P. Koestler, G. Poste, and R. G. Greig (1986) J. Biol. Chem. 261, 13,381). Here we report that antibody prepared against p32 p34 purified from human A375 melanoma cells immunoprecipitated an antigen of similar molecular mass from a panel of human, rat, and murine cells following challenge with sodium arsenite. No reactivity was observed in lysates from control, uninsulted cultures. The precise molecular mass of the arsenite-induced antigen was species-specific: 32 kDa (human and rat) and 34 kDa (murine). Indirect immunofluorescence analysis using affinity-purified monospecific IgG demonstrated that p32 p34 was localized to the cytoplasm and displayed a perinuclear distribution.

Original languageEnglish (US)
Pages (from-to)31-40
Number of pages10
JournalExperimental Cell Research
Issue number1
StatePublished - Sep 1988
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology


Dive into the research topics of 'Isolation and immunological characterization of the mammalian 32- 34-kDa stress protein'. Together they form a unique fingerprint.

Cite this