Characterization of a soluble form of dipeptidyl peptidase IV from pig liver

1983 ◽  
Vol 39 (9) ◽  
pp. 1005-1007 ◽  
Author(s):  
K. M. Fukasawa ◽  
K. Fukasawa ◽  
B. Y. Hiraoka ◽  
M. Harada
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Soluble Form ◽  
Pig Liver

Comparison of dipeptidyl peptidase IV prepared from pig liver and kidney

1981 ◽  
Vol 657 (1) ◽  
pp. 179-189 ◽  
Author(s):  
Kayoko M. Fukasawa ◽  
Katsuhiko Fukasawa ◽  
Bernard Y. Hiraoka ◽  
Minoru Harada
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Pig Liver ◽  
Liver And Kidney

scholarly journals Identification and characterization of a dipeptidyl peptidase IV inhibitor from aronia juice

2015 ◽  
Vol 465 (3) ◽  
pp. 433-436 ◽  
Author(s):  
Miyuki Kozuka ◽  
Takuya Yamane ◽  
Yoshihisa Nakano ◽  
Takenori Nakagaki ◽  
Iwao Ohkubo ◽  
...  
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Identification And Characterization

Purification and Characterization of Dipeptidyl Peptidase IV in Rat Liver Lysosomal Membranes1

1992 ◽  
Vol 111 (6) ◽  
pp. 770-777 ◽  
Author(s):  
Takahiro Kyouden ◽  
Masaru Himeno ◽  
Toyoko Ishikawa ◽  
Yukihide Ohsumi ◽  
Keitaro Kato
Keyword(s):  
Rat Liver ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Purification And Characterization

scholarly journals Biosynthesis of intestinal microvillar proteins. Pulse-chase labelling studies on maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV

1983 ◽  
Vol 210 (2) ◽  
pp. 389-393 ◽  
Author(s):  
E M Danielsen ◽  
H Sjöström ◽  
O Norén
Keyword(s):  
Organ Culture ◽  
Membrane Fraction ◽  
Bound State ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Soluble Form ◽  
Membrane Bound ◽  
Aminopeptidase A ◽  
High Mannose ◽  
Small Intestinal

The biogenesis of three intestinal microvillar enzymes, maltase-glucoamylase (EC 3.2.1.20), aminopeptidase A (aspartate aminopeptidase, EC 3.4.11.7) and dipeptidyl peptidase IV (EC 3.4.14.5), was studied by pulse-chase labelling of pig small-intestinal explants kept in organ culture. The earliest detectable forms of the enzymes were polypeptides of Mr 225000, 140000 and 115000 respectively. These were found to represent the enzymes in a ‘high-mannose’ state of glycosylation, as judged by their susceptibility to treatment with endo-beta-N-acetylglucosaminidase H (EC 3.2.1.96). After about 40-60 min of chase, maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV were further modified to yield the mature polypeptides of Mr 245000, 170000 and 137000 respectively, which were expressed at the microvillar membrane after 60-90 min of chase. The fact that the enzymes before reaching the microvillar membrane were found in a Ca2+-precipitated membrane fraction (intracellular and basolateral membranes), but not in soluble form, indicates that during biogenesis maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV are transported and assembled in a membrane-bound state.

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