2009
DOI: 10.1248/jhs.55.636
|View full text |Cite
|
Sign up to set email alerts
|

In Vitro Binding Assay of 31Methionine-oxidized Cholecystokinin Octapeptide to the CCKB Receptor

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

1
0
0

Year Published

2012
2012
2012
2012

Publication Types

Select...
1

Relationship

1
0

Authors

Journals

citations
Cited by 1 publication
(1 citation statement)
references
References 15 publications
1
0
0
Order By: Relevance
“…Recently, we reported that hydroxyl radicals could oxidize specifically 27 Met of glucagon (6), and furthermore that the ability of 27 Met sulfoxide of glucagon to produce cAMP was reduced to approximately 25% of that of native glucagon in HepG2 cells (6). A similar phenomenon has been observed in the case of cholecystokinin octapeptide (CCK8) (7), in which the oxidized CCK8 revealed in vitro-altered bioactivity in the LOVO cells (8). Similarly, oxidation of functionalized proteins or bioactive peptides by ROS could deteriorate their original and regular functions (9,10).…”
Section: Introductionsupporting
confidence: 55%
“…Recently, we reported that hydroxyl radicals could oxidize specifically 27 Met of glucagon (6), and furthermore that the ability of 27 Met sulfoxide of glucagon to produce cAMP was reduced to approximately 25% of that of native glucagon in HepG2 cells (6). A similar phenomenon has been observed in the case of cholecystokinin octapeptide (CCK8) (7), in which the oxidized CCK8 revealed in vitro-altered bioactivity in the LOVO cells (8). Similarly, oxidation of functionalized proteins or bioactive peptides by ROS could deteriorate their original and regular functions (9,10).…”
Section: Introductionsupporting
confidence: 55%