2006
DOI: 10.1042/bj20060079
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: 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 t… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
2

Citation Types

9
76
0
10

Year Published

2014
2014
2023
2023

Publication Types

Select...
6

Relationship

0
6

Authors

Journals

citations
Cited by 108 publications
(95 citation statements)
references
References 30 publications
9
76
0
10
Order By: Relevance
“…Since DPP9-S is known to form dimers, we asked whether DPP9-l behaves in a similar manner by comparing the elution profile of both enzymes on size exclusion chromatography. In line with previously published results [8,11,31], DPP9-S eluted from the gel filtration column in a single peak corresponding in size to a dimer (Fig. 2b).…”
Section: Dpp9-l Is An Active Peptidasesupporting
confidence: 92%
See 4 more Smart Citations
“…Since DPP9-S is known to form dimers, we asked whether DPP9-l behaves in a similar manner by comparing the elution profile of both enzymes on size exclusion chromatography. In line with previously published results [8,11,31], DPP9-S eluted from the gel filtration column in a single peak corresponding in size to a dimer (Fig. 2b).…”
Section: Dpp9-l Is An Active Peptidasesupporting
confidence: 92%
“…Importantly, DPP9-short was recently purified from bovine testes, confirming the endogenous expression of this short DPP9 isoform [34]. Bjelke et al [8] were the first to express a recombinant variant of the longer DPP9 form in insect cells (892 aa), and show that it is active. Surprisingly, in their study, the authors reported that the shorter DPP9 variant was inactive, suggesting that the N-terminal extension would affect the enzymatic activity of the peptidase.…”
Section: Introductionmentioning
confidence: 84%
See 3 more Smart Citations