ライフサイエンスコーパス: endoproteinase

1 al phosphopeptides upon treatment with lysyl endoproteinase.

2 e intracellular mammalian dibasic processing endoproteinases.

3 a combination of Asp-N and Glu-C (V8 strain) endoproteinases.

4 vitro proteolysis of human profilaggrin with endoproteinase 1 (PEP1), a protease involved in processi

5 assay (Endopep-MS) that detects the specific endoproteinase activities of all seven BoNT types by mas

6 CN) with an Aspergillus niger derived prolyl endoproteinase (An-PEP) for 1, 2, 3, 4, 8 and 24 h resul

7 ytic specificity of Aspergillus niger prolyl endoproteinase (An-PEP) on purified beta-casein (beta-CN

8 atrix metalloproteinases (MMPs), a family of endoproteinases, are implicated in cardiac remodeling.

9 was subsequently enzymatically digested with endoproteinase Arg C and separated by chromatography, wh

10 resist proteolysis by trypsin, chymotrypsin, endoproteinase Arg-C and endoproteinase Gluc-C.

11 lipid was cleaved by four enzymes: trypsin, endoproteinase Arg-C, endoproteinase Asp-N, and endoprot

12 at the amino-terminal pseudosubstrate by the endoproteinase Arg-C.

13 n against proteolysis catalyzed by mammalian endoproteinase Arg-C.

14 ease fragment decreased to 3.0 kDa while the endoproteinase ArgC fragment decreased to 3.2 kDa.

15 se fragment is Thr-173 to Glu-183, while the endoproteinase ArgC fragment is Val-178 to Arg-190.

16 e with Staphylococcus aureus V8 protease and endoproteinase ArgC yielded fragments of 8.2 and 9.0 kDa

17 ver, digestion of (32)PO(4)-labeled DAT with endoproteinase asp-N and immunoprecipitation with an N-t

18 ched to glass beads and further cleaved with endoproteinase Asp-N demonstrated that the labeled resid

19 gammaVal-102, whereas for the delta-subunit, endoproteinase Asp-N produced a labeled peptide beginnin

20 ry of the recombinant proteins digested with endoproteinase Asp-N revealed that disulfide pairing of

21 four enzymes: trypsin, endoproteinase Arg-C, endoproteinase Asp-N, and endoproteinase Glu-C.

22 MOA was digested with trypsin and endoproteinase Asp-N, and the peptide fragments were pur

23 ries of the PDZ domains after digestion with endoproteinase Asp-N, trypsin, and alpha-chymotrypsin.

24 Analysis of the endoproteinase Asp-N-generated carboxyl terminus of rhod

25 with trypsin, lysyl endopeptidase Lys-C, or endoproteinase Asp-N.

26 tment with a series of glycosidases and with endoproteinase Asp-N.

27 tibility of its C terminus to papain and the endoproteinase, Asp-N, followed by SDS/PAGE, which showe

28 Endoproteinase assays with gels containing incorporated

29 zyme is identified as C-terminal procollagen endoproteinase/bone morphogenetic protein-1 (BMP-1).

30 ntly fractionate the peptides resulting from endoproteinase digestion of 32P-labeled proteins.

31 through ion mobility and the use of multiple endoproteinase digestion significantly improved quantifi

32 man degradation, phosphoamino acid analysis, endoproteinase digestion, and mutagenesis of the SRC-1 p

33 Combined data from the tryptic and Glu-C endoproteinase digests of neuraminidase-inhibitor comple

34 de, and digested the latter with trypsin and endoproteinase Glu-C (EC 3.4.21.19).

35 Proteolysis by endoproteinase Glu-C (protease V8) reduces the Rrp1 prot

36 Proteolysis of corrin-labeled RTPR with endoproteinase Glu-C and peptide mapping at pH 5.8 revea

37 n was isolated by digesting the protein with endoproteinase Glu-C and purifying the N-terminal 1-55 p

38 ed from the lens sections were digested with endoproteinase Glu-C and subjected to mass spectrometric

39 recovered, and its further degradation with endoproteinase Glu-C established that cysteine-295 of al

40 d flavocytochrome b that had been exposed to endoproteinase Glu-C for 1 h.

41 ed by the demonstration that the radioactive endoproteinase Glu-C fragment derived from an A1 recepto

42 based on trypsin, endoproteinase Lys-C, and endoproteinase Glu-C increased this sequence coverage to

43 is of bacteriophage T7 primase/helicase with endoproteinase Glu-C produces several proteolytic fragme

44 The most sensitive sites for trypsin and endoproteinase Glu-C were observed in cbEGF-like motifs

45 s isolated; following partial digestion with endoproteinase Glu-C, an internal amino acid sequence wa

46 s for radiolabeled A1 receptor obtained with endoproteinase Glu-C, endoproteinase Lys-C, cyanogen bro

47 digested with formic acid, cyanogen bromide, endoproteinase Glu-C, or endoproteinase Lys-C, and the r

48 s particles became sensitive to digestion by endoproteinase Glu-C, providing further evidence of anti

49 An endoproteinase Glu-C-generated peptide had the predicted

50 red MAb was treated with trypsin followed by endoproteinase Glu-C.

51 oproteinase Arg-C, endoproteinase Asp-N, and endoproteinase Glu-C.

52 failed to inhibit the Staphylococcus aureus endoproteinase Glu-C.

53 digestion of the crude reaction mixture with endoproteinase Glu-C.

54 Sequential digestion with endoproteinase Glu-C/endoproteinase Lys-C limited the po

55 rst three predicted transmembrane spans, and endoproteinase Glu-C/trypsin digestion refined this pred

56 Digestion with endoproteinase GluC decreased the size of the radiolabel

57 6 and TMD 7-12 half-molecules, combined with endoproteinase GluC digestion, a substrate binding domai

58 In this study, we used trypsin and endoproteinase GluC to digest intact alpha-synuclein fib

59 psin, chymotrypsin, endoproteinase Arg-C and endoproteinase Gluc-C.

60 otein was confirmed by microsequencing of an endoproteinase glutamic acid-C fragment and by its abili

61 a defined hydrolysate sample, i.e. a prolyl endoproteinase hydrolysate of beta-casein and (c) short

62 1 is proteolytically processed by an unknown endoproteinase in planta.

63 a motif that was exceptionally resistant to endoproteinase K digestion.

64 esults of protease protection analysis using endoproteinase Lys-C and labeling of cysteine residues u

65 ubtype of purified mixed brain Gbetagamma by endoproteinase Lys-C blocks Gbetagamma-mediated stimulat

66 further refined to the first 16 residues by endoproteinase Lys-C cleavage and by cyanogen bromide cl

67 nstrated with the flowthrough fraction of an endoproteinase Lys-C digest of a recombinant immunoglobu

68 sequential exoglycosidase treatments of the endoproteinase Lys-C digest.

69 Analyses of trypsin and endoproteinase Lys-C digestion of 3-DAG-photolabeled GLU

70 th in terms of highest recoveries (including endoproteinase Lys-C digestions) and general applicabili

71 Partial proteolysis with endoproteinase Lys-C identified metal-stabilized fragmen

72 quential digestion with endoproteinase Glu-C/endoproteinase Lys-C limited the possible labeling to th

73 Endoproteinase Lys-C mapping of the position of the cros

74 y an accurate determination of the masses of endoproteinase Lys-C peptides using matrix-assisted lase

75 Digestion by endoproteinase Lys-C performed under nonreducing conditi

76 Applying limited proteolysis using endoproteinase Lys-C resulted in the predominant cleavag

77 Photolabeled CRABP-I was hydrolyzed with endoproteinase Lys-C to yield radioactive peptides, whic

78 Digestion of the mAb with endoproteinase Lys-C without disulfide scrambling was ac

79 Cleavage of photolabeled PGHS-1 with endoproteinase Lys-C yielded a peptide containing residu

80 gestion of SUMO(KGG) protein conjugates with endoproteinase Lys-C yields a diGly motif attached to ta

81 se of three enzyme digests based on trypsin, endoproteinase Lys-C, and endoproteinase Glu-C increased

82 ed by affinity chromatography, digested with endoproteinase Lys-C, and the peptide fragments analysed

83 , cyanogen bromide, endoproteinase Glu-C, or endoproteinase Lys-C, and the radio-labeled peptide(s) w

84 receptor obtained with endoproteinase Glu-C, endoproteinase Lys-C, cyanogen bromide, and hydroxylamin

85 ted by proteolytic treatment with trypsin or endoproteinase Lys-C, resulting in a stable cystine-knot

86 d secondary digestion of CNBr fragments with endoproteinase Lys-C.

87 additional proteolysis of this fragment with endoproteinase Lys-C.

88 4D3 from FRTL-5 cells was incubated with the endoproteinase Lys-C.

89 d subsequently digested by either trypsin or endoproteinase Lys-C.

90 Consecutive digestion with endoproteinase LysC and trypsin allows isolation of two

91 Endoproteinase LysC digestion of the cytosolic fraction

92 zymatic microreactors containing trypsin and endoproteinase LysC immobilized on a porous polymer mono

93 level, we found that the consecutive use of endoproteinases LysC and trypsin enabled identification

94 Endoproteinase lysine C digestion products of DGP were c

95 fact that it is hydrolyzed by many different endoproteinases, makes it suitable for many applications

96 a recombinant L3 23-kDa protein (recombinant endoproteinase (rEP)) expressed in Escherichia coli and

97 factor Xa, and the Bacillus subtilis dibasic endoproteinase subtilisin A through different mechanisms

98 Digestion of the protein with the endoproteinase subtilisin and analysis of products by li

99 ore closely mimics the natural substrates of endoproteinases, such as the calpains, than synthetic pe

100 atrix metalloproteinase (MMP) 10, a secreted endoproteinase that degrades the extracellular matrix.

101 prototypical mammalian kexin/subtilisin-like endoproteinase that is involved in the proteolytic proce

102 eptides from receptors digested with various endoproteinases were selectively isolated on immobilized

103 or, and lethal factor (LF), a zinc-dependent endoproteinase whose known targets include five members