Journal article
Intramolecular interactions in protein tyrosine phosphatase RPTPmu: kinetic evidence.
- Abstract:
-
The receptor-like protein tyrosine phosphatase RPTPmu contains three intracellular domains: the juxtamembrane (JM) and two phosphatase domains (D1 and D2). D1 is catalytically active in vitro. The functional roles of JM and D2 are still unclear. To find out whether and how they modulate the phosphatase activity of D1, we compared the enzymatic characteristics of two constructs, containing a truncated JM and either D1 or both phosphatase domains. p-Nitrophenyl phosphate and two peptide substra...
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- Publication status:
- Published
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- Publisher copy:
- 10.1006/bbrc.2000.4094
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Authors
Bibliographic Details
- Journal:
- Biochemical and biophysical research communications
- Volume:
- 280
- Issue:
- 1
- Pages:
- 319-327
- Publication date:
- 2001-01-01
- DOI:
- EISSN:
-
1090-2104
- ISSN:
-
0006-291X
- Source identifiers:
-
9163
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:9163
- UUID:
-
uuid:78c42a4b-1f60-48ec-bfd6-17303c7518c1
- Local pid:
- pubs:9163
- Deposit date:
- 2012-12-19
Terms of use
- Copyright date:
- 2001
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