Abstract:
:To evaluate the role of the sulphated tyrosine residue in position 27 in human cholecystokinin-33, parallel bioassay of the sulphated form of human cholecystokinin-33 and the unsulphated form of human cholecystokinin-33 was performed on the pancreatic protein secretion. Both peptides increased the protein output in a dose-related manner. However, the sulphated form possessed a considerably higher activity than the sulphated form. The relative potency of the unsulphated human cholecystokinin-33 compared to that of the sulphated human cholecystokinin-33 (taken as 1.0) was 0.08. From the results, it was suggested that the sulphated tyrosine may play an important role in controlling the activity of the longer molecular forms as well as that of the smaller forms of cholecystokinin.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Doi R,Inoue K,Kogire M,Sumi S,Yun M,Futaki S,Fujii N,Yajima H,Tobe Tdoi
10.1016/s0006-291x(88)81356-1subject
Has Abstractpub_date
1988-06-30 00:00:00pages
1209-13issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(88)81356-1journal_volume
153pub_type
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