Breakdown of N-terminally modified peptides and an isopeptide by rumen microorganisms.
AUTOR(ES)
Wallace, R J
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=182423Documentos Relacionados
- Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus
- Wnt signals are transmitted through N-terminally dephosphorylated β-catenin
- Negative regulation of STAT92E by an N-terminally truncated STAT protein derived from an alternative promoter site
- Duck Hepatitis B Virus Nucleocapsids Formed by N-Terminally Extended or C-Terminally Truncated Core Proteins Disintegrate during Viral DNA Maturation
- N-terminally myristoylated Ras proteins require palmitoylation or a polybasic domain for plasma membrane localization.
