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Immunological comparison of the coated vesicle H+-ATPases of plants and animals (1989)

Fichmann, Jenny ; Taiz, L. ; Gallagher, S. ; [et al.]

Springer

Protoplasma 153 (1989), S. 117-125

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ISSN: 1615-6102

Keywords: Vacuolar ATPase ; Plasma membrane ; Endomembrane ; Zucchini ; Brain

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary Polyclonal antibodies raised against the tonoplast and plasma membrane H+-ATPases of corn were used to probe Western blots lof clathrin-coated vesicles purified from zucchini hypocotyls and bovine brain. Antibodies to two tonoplast H+-ATPase subunits recognized their respective polypeptides in purified zucchini coated vesicle preparations. Antibody raised against the plasma membrane H+-ATPase failed to cross-react with zucchini coated vesicles, even though it recognized a 100 kDa polypeptide in purified zucchini plasma membrane preparations. These results suggest that zucchini coated vesicles contain a vacuolar-type rather than a plasma membrane-type H+-ATPase. Antibody to the corn 70 kDa subunit also cross-reacted with a 70 kDa band in bovine brain coated vesicle preparations. Surprisingly, the corn plasma membrane H+-ATPase antibody recognized a 100 kDa polypeptide in the bovine brain coated vesicle preparation. However, at least half of the 100 kDa antigen could be dissociated from the membrane by treatment with 2.0 M urea, indicating that it may represent one of the 100–110 kDa coat assembly proteins. A comparable protein appears to be absent from zucchini coated vesicles.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01322472

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Immobilized pH gradient two-dimensional gel electrophoresis and mass spectrometric identification of cytokine-regulated proteins in ME-180 cervical carcinoma cells (1997)

Matsui, Neil M. ; Smith, Diana M. ; Clauser, Karl R. ; [et al.]

Weinheim : Wiley-Blackwell

Electrophoresis 18 (1997), S. 409-417

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ISSN: 0173-0835

Keywords: Cervical carcinoma ; Two-dimensional polyacrylamide gel electrophoresis ; Mass spectrometry ; Immobilized pH gradient ; Cytokine ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology

Notes: Two-dimensional (2-D) polyacrylamide gel electrophoresis combined with mass spectrometry is a powerful combination of technologies that allows high resolution separation of proteins and their rapid identification. Immobilized pH gradient (IPG) first-dimensional gels have several advantages over carrier ampholyte isoelectric focusing, including a high degree of reproducibility, good protein spot resolution, and a selection of pH range. Here we demonstrate the utility and efficacy of combining IPG 2-D gel electrophoresis with mass spectrometry to identify interferon-γ- (IFN) and tumor necrosis factor (TNF)-regulated proteins in ME-180 cervical carcinoma cells. Three cytokine-regulated proteins have been identified, using imidazole-zinc-stained preparative IPG 2-D gels and in-gel tryptic digestion followed by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry for determination of peptide masses and sequences: (1) triosephosphate isomerase, a glycolytic pathway enzyme, (2) proteasome subunit C3, which is important in protein degradation, and (3) Ran, a GTP-binding protein important in cell cycle regulation, protein import into the nucleus, and RNA export from the nucleus.

Additional Material: 5 Ill.