Literature DB >> 3514791

Identity between cytoplasmic and membrane-bound S-100 proteins purified from bovine and rat brain.

R Donato, B Prestagiovanni, G Zelano.   

Abstract

Cytoplasmic and membrane-bound S-100 proteins were purified to homogeneity from bovine and rat brain. Cytoplasmic and membrane-bound S-100 from single species are identical by immunological, electrophoretic, spectrophotometric, and functional criteria. Cytoplasmic and membrane-bound S-100 from bovine brain consists of nearly equal amounts of S-100a and S-100b, whereas cytoplasmic and membrane-bound S-100 from rat brain consists mostly of S-100b. The functional role of membrane-bound S-100 remains to be elucidated.

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Year:  1986        PMID: 3514791     DOI: 10.1111/j.1471-4159.1986.tb01743.x

Source DB:  PubMed          Journal:  J Neurochem        ISSN: 0022-3042            Impact factor:   5.372


  3 in total

1.  Modifications of S100-protein immunoreactivity in rat brain induced by tissue preparation.

Authors:  M Rickmann; J R Wolff
Journal:  Histochem Cell Biol       Date:  1995-02       Impact factor: 4.304

2.  Glial cell differentiation in neuron-free and neuron-rich regions. II. Early appearance of S-100 protein positive astrocytes in human fetal hippocampus.

Authors:  M Stagaard Janas; R S Nowakowski; K Møllgård
Journal:  Anat Embryol (Berl)       Date:  1991

3.  Integration of proteomics, bioinformatics, and systems biology in traumatic brain injury biomarker discovery.

Authors:  J D Guingab-Cagmat; E B Cagmat; R L Hayes; J Anagli
Journal:  Front Neurol       Date:  2013-05-31       Impact factor: 4.003

  3 in total

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