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mascot protein identification program  (Matrix Science)
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Matrix Science mascot protein identification program
Characterization of permeabilized erythrocyte nuclei. (A) Proteins associated with Xenopus sperm, mouse sperm, and Xenopus erythrocyte nuclei. (B) Preparation of lysolecithin‐permeabilized nuclei from Xenopus laevis erythrocytes. (C) Proteins associated with permeabilized erythrocyte nuclei were analyzed by SDS‐PAGE and stained with Coomassie Blue (left). The gel was excised into small pieces and processed for LC–MS/MS analysis following in‐gel digestion with trypsin. To identify nucleus‐associated proteins, the mass spectra were analyzed using the <t>MASCOT</t> program and searched against <t>the</t> <t>PHROG</t> database. Identified proteins, together with their peptide counts and MASCOT scores, are shown (right). (D) Decreasing amounts of erythrocyte nuclei were analyzed by immunoblotting with antibodies against the indicated proteins. For semi‐quantitative comparison, mitotic egg extracts were analyzed on the same gel. (E) Erythrocyte nuclei were treated with increasing concentrations of micrococcal nuclease (MNase). The resulting DNA fragments were purified, separated on agarose gel, and visualized with ethidium bromide.
Mascot Protein Identification Program, supplied by Matrix Science, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Characterization of permeabilized erythrocyte nuclei. (A) Proteins associated with Xenopus sperm, mouse sperm, and Xenopus erythrocyte nuclei. (B) Preparation of lysolecithin‐permeabilized nuclei from Xenopus laevis erythrocytes. (C) Proteins associated with permeabilized erythrocyte nuclei were analyzed by SDS‐PAGE and stained with Coomassie Blue (left). The gel was excised into small pieces and processed for LC–MS/MS analysis following in‐gel digestion with trypsin. To identify nucleus‐associated proteins, the mass spectra were analyzed using the MASCOT program and searched against the PHROG database. Identified proteins, together with their peptide counts and MASCOT scores, are shown (right). (D) Decreasing amounts of erythrocyte nuclei were analyzed by immunoblotting with antibodies against the indicated proteins. For semi‐quantitative comparison, mitotic egg extracts were analyzed on the same gel. (E) Erythrocyte nuclei were treated with increasing concentrations of micrococcal nuclease (MNase). The resulting DNA fragments were purified, separated on agarose gel, and visualized with ethidium bromide.

Journal: Genes to Cells

Article Title: Histone Density and Dynamics Shape Mitotic Chromatid Architecture in Xenopus Egg Extracts

doi: 10.1111/gtc.70113

Figure Lengend Snippet: Characterization of permeabilized erythrocyte nuclei. (A) Proteins associated with Xenopus sperm, mouse sperm, and Xenopus erythrocyte nuclei. (B) Preparation of lysolecithin‐permeabilized nuclei from Xenopus laevis erythrocytes. (C) Proteins associated with permeabilized erythrocyte nuclei were analyzed by SDS‐PAGE and stained with Coomassie Blue (left). The gel was excised into small pieces and processed for LC–MS/MS analysis following in‐gel digestion with trypsin. To identify nucleus‐associated proteins, the mass spectra were analyzed using the MASCOT program and searched against the PHROG database. Identified proteins, together with their peptide counts and MASCOT scores, are shown (right). (D) Decreasing amounts of erythrocyte nuclei were analyzed by immunoblotting with antibodies against the indicated proteins. For semi‐quantitative comparison, mitotic egg extracts were analyzed on the same gel. (E) Erythrocyte nuclei were treated with increasing concentrations of micrococcal nuclease (MNase). The resulting DNA fragments were purified, separated on agarose gel, and visualized with ethidium bromide.

Article Snippet: Tandem mass spectra were analyzed using the MASCOT protein identification program (version 2.5.1; Matrix Science) and searched against the PHROG database (Wühr et al. ).

Techniques: SDS Page, Staining, Liquid Chromatography with Mass Spectroscopy, Western Blot, Comparison, Purification, Agarose Gel Electrophoresis