Chronic Obstructive Pulmonary Disease as a Main Factor of Premature Aging.

(1) Background: Chronic obstructive pulmonary disease (COPD) is defined as an inflammatory disorder that presents an increasingly prevalent health problem. Accelerated aging has been examined as a pathologic mechanism of many chronic diseases like COPD. We examined whether COPD is combined with accelerated aging, studying two hormones, dehydroepiandrosterone (DHEA) and growth hormone (GH), known to be characteristic biological markers of aging.

Identification of the 50S ribosomal proteins from the Eubacterium Thermus thermophilus.

The total protein mixture from the 50S subunit (TP-50) of the eubacterium Thermus thermophilus was characterized after blotting onto PVDF membranes from two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) and sequencing. The proteins were numbered according to their primary structure similarity with their counterparts from other species. One of them has been marked with an asterisk, namely L*23, because unlike the other known ribosomal proteins it shows a very low degree of homology.

Studies on the Zn-containing S14 ribosomal protein from Thermus thermophilus.

The S14 ribosomal protein from the thermophilic organism Thermus thermophilus, which contains a zinc-finger-like motif, namely -C-X2-C-X12-C-X2-C- [Tsiboli, P. & Choli, T. (1995) Biol.

Studies on S14 protein from Thermus thermophilus possessing zinc finger-like motifs.

The amino acid sequence of the ribosomal protein S14 of Thermus thermophilus has been determined both by automated sequence analysis of the intact protein as well as by DNA sequence analysis of the gene. The carboxy-terminal region was verified by both amino acid sequence analysis of the carboxy-terminal peptide produced after Glu-C digestion and by DNA sequence analysis. The protein contains 60 amino acid residues with a calculated molecular weight of 7008.

Purification and characterization of the 30S ribosomal proteins from the bacterium Thermus thermophilus.

The total protein mixture of the 30S subunit (TP-30) of the bacterium Thermus thermophilus has been purified using reverse-phase HPLC and the proteins obtained were identified both by means of two-dimensional polyacrylamide gel electrophoresis as well as by amino-terminal amino acid microsequence analysis. The proteins are numbered according to their primary structural similarity with known prokaryotic ribosomal proteins. Eight of them, namely proteins S6, S7, S9, S10, S14, S15, S16 and S17 run at different positions in the two-dimensional gel electrophoresis system to those suggested [Sedelnikova, S.