Human proteasome subunits from 2-dimensional gels identified by partial sequencing

P Kristensen; A H Johnsen; W Uerkvitz; K Tanaka; K B Hendil

doi:10.1006/bbrc.1994.2876

Human proteasome subunits from 2-dimensional gels identified by partial sequencing

Biochem Biophys Res Commun. 1994 Dec 30;205(3):1785-9. doi: 10.1006/bbrc.1994.2876.

Authors

P Kristensen¹, A H Johnsen, W Uerkvitz, K Tanaka, K B Hendil

Affiliation

¹ August Krogh Institute, University of Copenhagen, Denmark.

PMID: 7811265
DOI: 10.1006/bbrc.1994.2876

Abstract

Human proteasomes consist of 14 major subunits which can be resolved by two-dimensional polyacrylamide gel electrophoresis. Tryptic peptides from the subunits were sequenced. This allowed identification of all proteins in two-dimensional electrophoresis gels with proteasome subunits whose sequences are known from cDNA. The results also precisely define the specificity of a panel of subunit-specific monoclonal antibodies. A new proteasome subunit (Z) was discovered. In contrast, the putative subunit MECL-1 could not be detected in human placenta proteasomes.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Antibodies, Monoclonal
Cysteine Endopeptidases / chemistry*
Cysteine Endopeptidases / genetics
Cysteine Endopeptidases / isolation & purification
Electrophoresis, Gel, Two-Dimensional
Female
Humans
Molecular Sequence Data
Multienzyme Complexes / chemistry*
Multienzyme Complexes / genetics
Multienzyme Complexes / isolation & purification
Peptide Fragments / chemistry
Peptide Fragments / genetics
Peptide Fragments / immunology
Placenta / enzymology
Pregnancy
Proteasome Endopeptidase Complex
Protein Conformation
Sequence Homology, Amino Acid

Substances

Antibodies, Monoclonal
Multienzyme Complexes
Peptide Fragments
Cysteine Endopeptidases
Proteasome Endopeptidase Complex