Breakdown of N-terminally modified peptides and an isopeptide by rumen microorganisms.
Treatment of Trypticase peptides with acetic anhydride, succinic anhydride, or maleic anhydride inhibited their breakdown to ammonia by rumen microorganisms by an average of 89% after 12 h of incubation in vitro. All three treatments gave similar protection. Acetylation also protected dipeptides containing lysine and methionine from degradation. However, more effective protection was obtained by linking lysine and methionine as N-epsilon-methionyl lysine.
Wallace
R J
RJ
Rowett Research Institute, Bucksburn, Aberdeen, United Kingdom.
Frumholtz
P P
PP
Walker
N D
ND
D000089:Acetic Anhydrides; D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins; D004151:Dipeptides / Q000737:chemistry / Q000378:metabolism; D008299:Maleic Anhydrides; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011492:Protein Hydrolysates; D012417:Rumen / Q000382:microbiology*; D012756:Sheep; D013387:Succinic Anhydrides
D000089:Acetic Anhydrides; D002364:Caseins; D004151:Dipeptides; D008299:Maleic Anhydrides; D010455:Peptides; D011492:Protein Hydrolysates; D013387:Succinic Anhydrides; C026375:trypticase-soy broth; C031800:acetic anhydride; C031801:succinic anhydride