Phosphoamino acids in proteasome subunits. 1996

A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
Diabetes Forschunginstitut, Düsseldorf, Germany.

Proteasomes, the major catalysts of the non-lysosomal proteolytic pathway in eukaryotic cells, were analyzed for their content of phosphoamino acids using polyacrylamide gel electrophoresis and subsequent detection on Western blots by phosphoamino acid antibodies. No specific binding to proteasome subunits was observed with phosphoserine or phosphothreonine antibodies, whereas phosphotyrosine antibodies were bound by a single proteasome subunit, which was identified in rat as well as in human proteasomes as subunit C7-1. Since dephosphorylation of the subunit by phosphatases was not possible, analysis of phosphoamino acid content of all proteasome subunits was performed using another method. All proteasome subunits were isolated from 2D-polyacrylamide gels and subjected to partial acid hydrolysis. Phosphoamino acids were subsequently detected by capillary electrophoresis after their derivatization with phenylisothiocyanate. This analysis revealed no phosphorylated amino acid in subunit C7-1, however, subunit C3 contained phosphotyrosine and phosphothreonine, and phosphoserine was detected in subunits zeta, C5, C8 and C9.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D010449 Peptide Mapping Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases. Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D015180 Electrophoresis, Gel, Two-Dimensional Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels. Gel Electrophoresis, Two-Dimensional,Polyacrylamide Gel Electrophoresis, Two-Dimensional,2-D Gel Electrophoresis,2-D Polyacrylamide Gel Electrophoresis,2D Gel Electrophoresis,2D PAGE,2D Polyacrylamide Gel Electrophoresis,Electrophoresis, Gel, 2-D,Electrophoresis, Gel, 2D,Electrophoresis, Gel, Two Dimensional,Polyacrylamide Gel Electrophoresis, 2-D,Polyacrylamide Gel Electrophoresis, 2D,Two Dimensional Gel Electrophoresis,2 D Gel Electrophoresis,2 D Polyacrylamide Gel Electrophoresis,Electrophoresis, 2-D Gel,Electrophoresis, 2D Gel,Electrophoresis, Two-Dimensional Gel,Gel Electrophoresis, 2-D,Gel Electrophoresis, 2D,Gel Electrophoresis, Two Dimensional,PAGE, 2D,Polyacrylamide Gel Electrophoresis, 2 D,Polyacrylamide Gel Electrophoresis, Two Dimensional,Two-Dimensional Gel Electrophoresis
D017208 Rats, Wistar A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain. Wistar Rat,Rat, Wistar,Wistar Rats
D046988 Proteasome Endopeptidase Complex A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme. 20S Proteasome,Ingensin,Macropain,Macroxyproteinase,Multicatalytic Endopeptidase Complex,Multicatalytic Proteinase,Prosome,Proteasome,Complex, Multicatalytic Endopeptidase,Complex, Proteasome Endopeptidase,Endopeptidase Complex, Multicatalytic,Endopeptidase Complex, Proteasome,Proteasome, 20S,Proteinase, Multicatalytic

Related Publications

A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
March 2012, Organic letters,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
May 1998, Journal of chromatography. A,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
July 1982, Analytical biochemistry,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
July 1999, BioTechniques,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
February 2005, Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
January 2021, Archives of medical research,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
April 1991, Journal of biochemistry,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
May 1995, Analytical biochemistry,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
March 1997, Molecular biology reports,
A Wehren, and H E Meyer, and A Sobek, and P M Kloetzel, and B Dahlmann
April 2003, Biochemical Society transactions,
Copied contents to your clipboard!