Dipeptidyl Peptidase IV from Xanthomonas maltophilia: Sequencing and Expression of the Enzyme Gene and Characterization of the Expressed Enzyme

1996 ◽  
Vol 120 (6) ◽  
pp. 1111-1117 ◽  
Author(s):  
T. Kabashima ◽  
K. Ito ◽  
T. Yoshimoto
Keyword(s):  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Enzyme Gene ◽  
Xanthomonas Maltophilia ◽  
Sequencing And Expression

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 Dipeptidyl peptidases 8 and 9: specificity and molecular characterization compared with dipeptidyl peptidase IV

2006 ◽  
Vol 396 (2) ◽  
pp. 391-399 ◽  
Author(s):  
Jais R. Bjelke ◽  
Jesper Christensen ◽  
Per F. Nielsen ◽  
Sven Branner ◽  
Anders B. Kanstrup ◽  
...  
Keyword(s):  
Peptide Yy ◽  
Expression System ◽  
Baculovirus Expression System ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Dipeptidyl Peptidases ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1 ◽  
Dipeptidyl Peptidase Iv Inhibition

Dipeptidyl peptidases 8 and 9 have been identified as gene members of the S9b family of dipeptidyl peptidases. In the present paper, we report the characterization of recombinant dipeptidyl peptidases 8 and 9 using the baculovirus expression system. We have found that only the full-length variants of the two proteins can be expressed as active peptidases, which are 882 and 892 amino acids in length for dipeptidyl peptidase 8 and 9 respectively. We show further that the purified proteins are active dimers and that they show similar Michaelis–Menten kinetics and substrate specificity. Both cleave the peptide hormones glucagon-like peptide-1, glucagon-like peptide-2, neuropeptide Y and peptide YY with marked kinetic differences compared with dipeptidyl peptidase IV. Inhibition of dipeptidyl peptidases IV, 8 and 9 using the well-known dipeptidyl peptidase IV inhibitor valine pyrrolidide resulted in similar Ki values, indicating that this inhibitor is non-selective for any of the three dipeptidyl peptidases.

Generation and characterization of dipeptidyl peptidase-IV inhibitory peptides from trypsin-hydrolyzed α-lactalbumin-rich whey proteins

2020 ◽  
Vol 318 ◽  
pp. 126333 ◽  
Author(s):  
Cheng-li Jia ◽  
Naveed Hussain ◽  
Obaroakpo Joy Ujiroghene ◽  
Xiao-yang Pang ◽  
Shu-wen Zhang ◽  
...  
Keyword(s):  
Whey Proteins ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv ◽  
Inhibitory Peptides

Biochemical characterization of CD26 (dipeptidyl peptidase IV): Functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies

1992 ◽  
Vol 29 (2) ◽  
pp. 183-192 ◽  
Author(s):  
Yoshihiro Torimoto ◽  
Nam H. Dang ◽  
Toshiaki Tanaka ◽  
Catherine Prado ◽  
Stuart F. Schlossman ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Biochemical Characterization ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase Iv
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