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G W Welling

Publications and source records attributed to G W Welling.

120 records · Page 7Linked to original sources
PubMed1976

Studies on the primary structure of bison pancreatic ribonuclease.

Bison pancreatic ribonuclease was isolated by affinity chromatography. Thermolysin and tryptic digestion of denaturated protein, and subtilisin digestion of native protein yielded peptides, which were purified and submitted to amino acid analysis. These peptides, together with partial sequence data obtained by Stewart & Stevenson (16) overlap the entire amino acid sequence of bison ribonuclease. No differences with bovine ribonuclease were found, although there may be differences in state of amidation of some residues.

Amino Acid Sequence↗
PubMed1975

The amino acid sequence of dromedary pancreatic ribonuclease.

Dromedary (Camelus dromedarius) RNAase (ribonuclease) was isolated from pancreatic tissue by affinity chromatography. Peptides obtained by digestion with different proteolytic enzymes and CNBr were isolated by gel filtration, preparative high-voltage paper electrophoresis and paper chromatography. Peptides were sequenced by the dansyl-Edman method. All peptide bonds were overlapped by one or more peptides. The polypeptide chain consists of 123 amino acids. A deletion (position 39) was observed in an external loop of the polypeptide chain (residues 35-40), as was found earlier to horse RNAase (Scheffer & Beintema, 1974). A heterogeneity was found at position 103 (glutamine and lysine). Dromedary RNAase differs at 23-32% of the positions from all other pancreatic RNAases sequenced to date. In evolutionary terms this indicates that dromedary RNAase has evolved independently during the larger part of the evolution of the mammals. Detailed evidence for the sequence has been deposited as Supplementary Publication SUP 50046 (14 pages) at the British Library (Lending Division), Boston Spa, Wetherby, W. Yorks. LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem. J. (1975) 145, 5.

Amino Acid Sequence↗
PubMedDate not supplied

The effect of ceftriaxone on the anaerobic bacterial flora and the bacterial enzymatic activity in the intestinal tract.

The normal flora of the intestinal tract, mainly consisting of anaerobic bacteria, protects the host against colonization by pathogenic microorganisms. Antimicrobial treatment with ceftriaxone may influence the colonic microflora and as a consequence, the protective effect. Ten healthy volunteers received 1 g of ceftriaxone intramuscularly for five days. This resulted in a significant decrease (p less than 0.05) of the mean cultural counts (+/- SEM) of total anaerobes from 10.67 (0.11) (prior to treatment) to 9.02 (0.45) and 8.97 (0.46) at days 3 and 5, respectively (during treatment). After treatment (days 10 and 15-19), the cultural counts of anaerobes returned to 10.17 (0.16) and 10.44 (0.18), respectively. Bacterial enzymes may serve as an indicator of protective microflora. beta- aspartylpeptidase and deoxycholate hydrolase activity was determined in faecal supernatants of the volunteers and compared with anaerobic culturing. Both enzymatic activities show a significant correlation with the total number of anaerobes present at day 3 of deftriaxone treatment. At day 5 and 8 only beta-aspartylpeptidase showed significant correlations with cultural counts of total anaerobes, Bacteroides spp. or bifidobacteria. At day 15 to 19 (ten to 14 days after treatment) beta-aspartylpeptidase showed only a significant correlation with the number of Bacteroides spp. This indicates that changes in the indigenous bacterial flora during and shortly after treatment with ceftriaxone can be monitored by determination of beta-aspartylpeptidase. Recovery of the intestinal flora is difficult to assess in this manner.

Adult↗
PubMedDate not supplied

Enzymatic inactivation of aztreonam by faecal enzyme preparations from healthy volunteers.

The enzymatic inactivation of aztreonam by the faecal flora was investigated in 25 healthy human volunteers. Ten volunteers received aztreonam orally and 15 volunteers did not receive antibiotic treatment. Residual aztreonam and its inactivated open ring form were simultaneously detected by an HPLC-assay. Independent of aztreonam treatment, beta-lactamase activity was detected in the faecal flora of 20 volunteers. The inactivation of aztreonam by the faecal supernatants was inhibited by clavulanic acid.

Adult↗