Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0267964 (PAA)
 2,561 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isolated and highly purified myeloma IgD DEK, STA and SAR were subjected to isoelectric focusing in thin layer of polyacrylamide gel using equipment and PAG plate 3, 5-10 from LKB. Although homogeneous in electrophoresis on cellulose acetate folien, immunoelectrophoresis and DISC PAA gel electrophoresis analysed IgD showed high isoelectric heterogeneity. They formed isoelectric spectra with 24-27 pl zonnes ower the pH range 5,4-9,3. Based on densitometric analysis of gel stripps zonnes with a small protein content were excluded from calculation of the real isoelectrical range. According to that manipulation isoelectrical range was determined as pH 6-8. Heterogeneity of isolated myeloma IgD may be due to the post-synthetic transformation of molecules in vivo as well to degradation and/or aggregation of IgD in vitro during the preparation of samples for isoelectrofocusing. However, myeloma IgD are in fact more heterogeneous in isoelectrofocusing than myeloma immunoglobulins of other classes.
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PMID:[Isoelectric spectrum of IgD in myeloma]. 26 66

The 20S proteasome is the proteolytic complex in eukaryotes responsible for degrading short-lived and abnormal intracellular proteins, especially those targeted by ubiquitin conjugation. The 700-kD complex exists as a hollow cylinder comprising four stacked rings with the catalytic sites located in the lumen. The two outer rings and the two inner rings are composed of seven different alpha and beta polypeptides, respectively, giving an alpha7/beta7/beta7/alpha7 symmetric organization. Here we describe the molecular organization of the 20S proteasome from the plant Arabidopsis thaliana. From an analysis of a collection of cDNA and genomic clones, we identified a superfamily of 23 genes encoding all 14 of the Arabidopsis proteasome subunits, designated PAA-PAG and PBA-PBG for Proteasome Alpha and Beta subunits A-G, respectively. Four of the subunits likely are encoded by single genes, and the remaining subunits are encoded by families of at least 2 genes. Expression of the alpha and beta subunit genes appears to be coordinately regulated. Three of the nine Arabidopsis proteasome subunit genes tested, PAC1 (alpha3), PAE1 (alpha5) and PBC2 (beta3), could functionally replace their yeast orthologs, providing the first evidence for cross-species complementation of 20S subunit genes. Taken together, these results demonstrate that the 20S proteasome is structurally and functionally conserved among eukaryotes and suggest that the subunit arrangement of the Arabidopsis 20S proteasome is similar if not identical to that recently determined for the yeast complex.
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PMID:Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana. 961 Nov 83