Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Alfred Jann"'
Autor:
Florence Rochat, Etienne Pouteau, Kurt Ornstein, Bruce German, Olivier Ballevre, Alfred Jann, Isabelle Meirim, Jose L. Sanchez-Garcia
Chicory roots are rich in inulin that is degraded into SCFA in the caecum and colon. Whole-body SCFA metabolism was investigated in rats during food deprivation and postprandial states. After 22 h of food deprivation, sixteen rats received an IV inje
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c1806f4d559467db90c506cc3bac285
http://doc.rero.ch/record/302831/files/S0007114507815790.pdf
http://doc.rero.ch/record/302831/files/S0007114507815790.pdf
Autor:
Alfred Jann, Patricia A. Judd, Kevin Whelan, Moira A. Taylor, Rainer Simmering, Victor R. Preedy
Publikováno v:
The Journal of Nutrition. 135:1896-1902
The intestinal microbiota are important during enteral tube feeding because they exert colonization resistance and produce SCFAs. However, the effect of the enteral formula composition on major bacterial groups of the microbiota has not been clearly
Publikováno v:
Glycobiology. 19(12)
Old age is linked to numerous changes of body functions such as salivation, gastrointestinal motility, and permeability all linked to central and enteric nervous system decline. Thus, gut motility and barrier functions suffer. Sialic acid plays a key
Autor:
Jean-Richard Neeser, Alfred Jann, Daniel Schmid, Guido Capitani, David Pridmore, Roberto Battistutta
Publikováno v:
FEBS Letters, Vol. 414, No 3 (1997) pp. 590-594
A new ice nucleation gene from Pseudomonas syringae was isolated and overexpressed as a fully active protein in Escherichia coli in order to gain experimental data about the structure of ice nucleation proteins. No evidence of a signal sequence or se
Publikováno v:
Proceedings of the National Academy of Sciences. 83:4937-4941
Arginine-nonutilizing ( aru ) mutants of Pseudomonas aeruginosa strain PAO converted L-arginine to N 2 -succinylarginine or N -succinylglutamate, which were identified by high-voltage electrophoresis and HPLC. Addition of aminooxyacetate, an inhibito
Publikováno v:
Microbiology. 134:1043-1053
SUMMARY: D-Arginine dehydrogenase activity was discovered in Pseudomonas aeruginosa. This enzyme was inducible by its substrate, D-arginine, as well as by its product, 2-ketoarginine, but not by L-arginine. The enzyme activity was measured in vitro,
Publikováno v:
Archives of microbiology. 150(4)
Most Pseudomonas aeruginosa PAO mutants which were unable to utilize l-arginine as the sole carbon and nitrogen source (aru mutants) under aerobic conditions were also affected in l-ornithine utilization. These aru mutants were impaired in one or sev