Neuroglobin and cytoglobin, members of the globin family, are present in vertebrate cells at very low concentrations. As the function of both proteins is still a matter of debate, it is very important to be able to produce and purify these proteins, and in general all members of the globin family, to homogeneity. For this purpose, this chapter describes the expression of neuro- and cytoglobin by E. coli and its preparative purification. These proteins are then used in crystallization experiments. Also an analytical purification strategy is discussed in detail.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/S0076-6879(08)36019-4 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Impaired hypoxic tolerance in APP23 mice: a dysregulation of neuroprotective globin levels.
FEBS Lett
May 2017
Laboratory of Protein Science, Proteomics and Epigenetic Signalling, Department of Biomedical Sciences, University of Antwerp, Wilrijk, Belgium.
Although neuroglobin confers neuroprotection against Alzheimer's disease (AD) pathology, its expression becomes downregulated in late-stage AD. Here, we provide evidence that indicates that this decrease is associated with the AD-linked angiopathy. While wild-type mice of different ages show upregulated cerebral neuroglobin expression upon whole-body hypoxia, APP23 mice exhibit decreased cerebral transcription of neuroglobin.
View Article and Find Full Text PDFNeurons express hemoglobin alpha- and beta-chains in rat and human brains.
J Comp Neurol
August 2009
Department of Neurology, David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, California 90095, USA.
Hemoglobin is the oxygen carrier in vertebrate blood erythrocytes. Here we report that hemoglobin chains are expressed in mammalian brain neurons and are regulated by a mitochondrial toxin. Transcriptome analyses of laser-capture microdissected nigral dopaminergic neurons in rats and striatal neurons in mice revealed the presence of hemoglobin alpha, adult chain 2 (Hba-a2) and hemoglobin beta (Hbb) transcripts, whereas other erythroid markers were not detected.
View Article and Find Full Text PDFExpression, purification, and crystallization of neuro- and cytoglobin.
Methods Enzymol
May 2008
Department of Biomedical Sciences, University of Antwerp, Antwerp, Belgium.
Neuroglobin and cytoglobin, members of the globin family, are present in vertebrate cells at very low concentrations. As the function of both proteins is still a matter of debate, it is very important to be able to produce and purify these proteins, and in general all members of the globin family, to homogeneity. For this purpose, this chapter describes the expression of neuro- and cytoglobin by E.
View Article and Find Full Text PDFThe possible enzymatic activities of neuro- and cytoglobin as well as their potential function as substrates in enzymatic reactions were studied. Neuro- and cytoglobin are found to show no appreciable superoxide dismutase, catalase, and peroxidase activities. However, the internal disulfide bond (CD7-D5) of human neuroglobin can be reduced by thioredoxin reductase.
View Article and Find Full Text PDFGenomic organization and mutation analysis of three candidate genes for hereditary neuralgic amyotrophy.
Muscle Nerve
April 2004
Department of Neurology, University of Münster, Albert Schweitzer Strasse 33, 48129 Münster, Germany.
Hereditary neuralgic amyotrophy (HNA) is an autosomal-dominant inherited recurrent focal neuropathy affecting mainly the brachial plexus. In this study we report the genomic structure and mutation analysis of three candidate genes: sphingosine kinase 1 (SPHK1); tissue inhibitor of metalloproteinase 2 (TIMP2); and cytoglobin (CYGB). We did not find any disease-associated mutations, indicating that HNA is not caused by point mutations in these genes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!