In:
Biochemical Journal, Portland Press Ltd., Vol. 258, No. 1 ( 1989-02-15), p. 305-308
Abstract:
Inhibitor studies were performed on the two endopeptidase activities involved in proinsulin conversion in isolated insulin secretory granules [Davidson, Rhodes & Hutton (1988) Nature (London) 333, 93-96]. The active-site-directed peptides L-alanyl-L-arginyl-L-arginylmethyldimethylsulphonium and L-alanyl-L-lysyl-L-arginylmethyldimethylsulphonium inhibited these activities in accordance with the observed cleavage pattern, su ggesting that the primary amino acid sequence of the dibasic site was an important determinant of the endopeptidase substrate specificities.
Type of Medium:
Online Resource
ISSN:
0264-6021
,
1470-8728
Language:
English
Publisher:
Portland Press Ltd.
Publication Date:
1989
detail.hit.zdb_id:
1473095-9
SSG:
12
