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

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

Research output: Contribution to journalArticle

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Abstract

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
Volume178
Issue number1
DOIs
StatePublished - 1988
Externally publishedYes

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Heat-Shock Proteins
Antigens
Indirect Fluorescent Antibody Technique
Heavy Metals
Melanoma
Cytoplasm
Immunoglobulin G
Antibodies
sodium arsenite

ASJC Scopus subject areas

  • Cell Biology

Cite this

Isolation and immunological characterization of the mammalian 32- 34-kDa stress protein. / Caltabiano, Madelyn M.; Poste, George; Greig, Russell G.

In: Experimental Cell Research, Vol. 178, No. 1, 1988, p. 31-40.

Research output: Contribution to journalArticle

Caltabiano, Madelyn M. ; Poste, George ; Greig, Russell G. / Isolation and immunological characterization of the mammalian 32- 34-kDa stress protein. In: Experimental Cell Research. 1988 ; Vol. 178, No. 1. pp. 31-40.
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