ライフサイエンスコーパス: carboxypeptidase B

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1 ased from the C-terminus of mZP2 and mZP3 by carboxypeptidase B.

2 idues in HPRG, and by treatment of HPRG with carboxypeptidase B.

3 bomodulin complex activated all the mutants, carboxypeptidase B activity of the activated mutants aga

4 llowed detection limits of 1-2 pM enzyme for carboxypeptidase B and activated thrombin-activatable fi

5 carboxypeptidase-U, carboxypeptidase-R, pro-carboxypeptidase-B, and thrombin-activatable fibrinolysi

6 mZP2 and mZP3, Arg residues were released by carboxypeptidase B, consistent with processing at the co

7 HTRF) assay has been developed for measuring carboxypeptidase B (CPB) activity in a miniaturized high

8 Thrombin-activatable carboxypeptidase B (CPB), also called thrombin-activatab

9 Plasma carboxypeptidase B (CPB), which is activated by the thro

10 surface and are sensitive to proteolysis by carboxypeptidase B (CpB).

11 to 2.05-A resolution and demonstrate robust carboxypeptidase B-like activity for the enzyme.

12 n be activated by thrombin to an enzyme with carboxypeptidase B-like activity.

13 After release of FPB a carboxypeptidase-B-like enzyme removes the carboxyl-term

14 Plasma carboxypeptidase B (PCB) is an exopeptidase that exerts

15 The ability of plasma carboxypeptidase B (pCPB) to remove these residues sugge

16 the crystal structure of porcine pancreatic carboxypeptidase B (pp-CpB) in complex with a variety of

17 Da glycosylated carboxypeptidase, plasma pro-carboxypeptidase B (pro-plasma CPB), has recently been i

18 ment of the Cpefat/Cpefat brain extract with carboxypeptidase B restores the level of Leu-enkephalin

19 s B, C and F bound to the surrogate protease carboxypeptidase B revealed the binding modes of these l

20 ral product inhibitors in a modified porcine carboxypeptidase B revealed their binding mode and provi

21 Carboxypeptidase B-sensitive plasminogen binding sites p

22 pped forms, the sample is treated first with carboxypeptidase B to reduce the charge microheterogenei

23 The cap is subsequently removed with carboxypeptidase B to yield mature biologically active I

24 ys]Pg activation kinetics with wild-type SK, carboxypeptidase B-treated SK, and a COOH-terminal Lys41

25 Carboxypeptidase B treatment decreased cell-dependent pl

26 Carboxypeptidase B treatment eliminated the increment in

27 ean trypsin inhibitor and was susceptible to carboxypeptidase B treatment, implicating proteolysis an

28 the enzymatic activity and concentration of Carboxypeptidase B was developed.

29 ombining targeted specific proteolysis using carboxypeptidase B with a proteomics approach using two-

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