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  The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme

Dahlmann, B., Kopp, F., Kühn, L., Hegerl, R., Pfeifer, G., & Baumeister, W. (1991). The multicatalytic proteinase (prosome, proteasome): comparison of the eukaryotic and archaebacterial enzyme. Biomedica Biochimica Acta., 50(4-6), 465-469.

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Dahlmann, B., Author
Kopp, F., Author
Kühn, L., Author
Hegerl, R.1, Author              
Pfeifer, G.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Amino Acid Sequence; Animal; Binding Sites; Comparative Study; Cysteine Endopeptidases/ch [Chemistry]; *Cysteine Endopeptidases/me [Metabolism]; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes/ch [Chemistry]; *Multienzyme Complexes/me [Metabolism]; Muscles/en [Enzymology]; Oligopeptides/ch [Chemistry]; Protein Conformation; Rats; Species Specificity; Substrate Specificity; *Thermoplasma/en [Enzymology]
 Abstract: Proteasomes isolated and purified from rat muscle tissue and from the archaebacterium Thermoplasma acidophilum have a very similar size and shape, but the subunit composition is less complex in the archaebacterium as compared to the eukaryotic particle. The archaebacterial enzyme contains a catalytic site with chymotryptic specificity, which is inhibited by serine proteinase inhibitors and clearly differs from the eukaryotic particle which has a minimum of three catalytic sites for peptide bond hydrolysis of a yet undefined mechanism.

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 Dates: 1991
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: eDoc: 318353
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Title: Biomedica Biochimica Acta.
Source Genre: Journal
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Pages: - Volume / Issue: 50 (4-6) Sequence Number: - Start / End Page: 465 - 469 Identifier: -