ライフサイエンスコーパス: proteolytic digestion

1 second alkylation was carried out during the proteolytic digestion.

2 idue Rel(Seq) protein are defined by limited proteolytic digestion.

3 fragments resulting from partial or complete proteolytic digestion.

4 as localized to the amino-terminal domain by proteolytic digestion.

5 omplished simply by washing the gel prior to proteolytic digestion.

6 an altered conformation detectable by Glu-C proteolytic digestion.

7 DS-PAGE, Ni(2+) affinity chromatography, and proteolytic digestion.

8 tein aggregates resistant to degradation and proteolytic digestion.

9 near the zinc ligands becomes accessible to proteolytic digestion.

10 sed resistance of the full-length protein to proteolytic digestion.

11 idues, the modified protein was subjected to proteolytic digestion.

12 e fluorescent probe 1,8-ANS, and (3) limited proteolytic digestion.

13 lex into three protein components by limited proteolytic digestion.

14 nding on the peptides that are formed during proteolytic digestion.

15 as previously shown, but also the pattern of proteolytic digestion.

16 y are unstable and undergo hydrolysis during proteolytic digestion.

17 lots and thrombi are stable structures until proteolytic digestion.

18 ficulty in achieving complete and consistent proteolytic digestion.

19 tochondrial DNA helicase more susceptible to proteolytic digestion.

20 complete, including the incubation time for proteolytic digestion.

21 rmediates at <0.007 Da mass accuracy without proteolytic digestion.

22 ither partial unfolding of the enzyme or its proteolytic digestion.

23 xhibit improved regularity and resistance to proteolytic digestion.

24 lization of structural modifications without proteolytic digestion.

25 e of S. mutans alters P1's susceptibility to proteolytic digestion.

26 ition and confers the ECM with resistance to proteolytic digestion.

27 n (HSA) by online EC reduction of nonreduced proteolytic digestions.

28 greater protein instability in chymotrypsin proteolytic digestions.

29 form infrared and NMR spectroscopies, and by proteolytic digestions.

30 d software tool for evaluating and comparing proteolytic digestion across diverse experimental condit

31 nderwent in vitro simulated gastrointestinal proteolytic digestion after a wide range of thermal trea

32 the total CE protein could be solubilized by proteolytic digestion after saponification, of which inv

33 Proteolytic digestion analysis demonstrates A domain mov

34 A combination of proteolytic digestion and affinity-directed mass spectro

35 sensitive protein identification by on-line proteolytic digestion and analysis of protein digests us

36 ation sites in human NF-H were identified by proteolytic digestion and analysis of the resulting dige

37 hich was confirmed experimentally by limited proteolytic digestion and competitive ligand-binding ass

38 EM analysis, combined with proteolytic digestion and deletion mapping, revealed the

39 demonstrated by increased susceptibility to proteolytic digestion and enhanced susceptibility to unf

40 turized trypsin-membrane reactor for on-line proteolytic digestion and ESI-MS analysis for protein/pe

41 A simultaneous on-tissue proteolytic digestion and extraction method is described

42 Conformational changes probed by proteolytic digestion and fluorescence signal reported b

43 omponents that restricted AdV access because proteolytic digestion and inhibitors of O-linked glycosy

44 terized by mass spectrometric analysis after proteolytic digestion and isolation of fluorescent photo

45 In-gel proteolytic digestion and LC-MS/MS analysis were conduct

46 c analysis of complex protein mixtures using proteolytic digestion and liquid chromatography in combi

47 l acetyl phosphate (MAP) in combination with proteolytic digestion and mass spectral analysis show th

48 as well as proteins in gel slices, prior to proteolytic digestion and mass spectral analysis.

49 Proteolytic digestion and mass spectrometric analysis in

50 Chemical cross-linking combined with proteolytic digestion and mass spectrometry (MS) is a pr

51 continuous labeling experiment, followed by proteolytic digestion and MS analysis, generates a large

52 Utilizing proteolytic digestion and nano-LC-MS/MS analysis, we con

53 Mn2+ increased the resistance of HIV-1 IN to proteolytic digestion and produced a digestion pattern t

54 Proteolytic digestion and protein kinase protection expe

55 ely on multi-step enzymatic assays requiring proteolytic digestion and separate quantification of GHS

56 units, p42 and p22, was determined following proteolytic digestion and sequence analysis of the resul

57 ch Edman sequencing, amino acid analysis, or proteolytic digestion and sequencing by tandem mass spec

58 e presence of [32P]ATP, prior to solid-phase proteolytic digestion and two-dimensional phosphopeptide

59 onformational stability, high sensitivity to proteolytic digestion, and a replication rate of 10(6)-f

60 ks such as poor absorption, low stability to proteolytic digestion, and fast clearance.

61 le quantum coherence (HSQC) spectra, limited proteolytic digestion, and fluorescence data suggest tha

62 the elongating new peptide, protect it from proteolytic digestion, and guide its emergence.

63 the Fl(N5[O]) species via isotope labeling, proteolytic digestion, and high-resolution tandem mass s

64 characterize because of their resistance to proteolytic digestion, and knowledge of the precise posi

65 sed a combination of chemical cross-linking, proteolytic digestion, and mass spectrometry (MALDI-TOF

66 combination of hydrogen/deuterium exchange, proteolytic digestion, and mass spectrometry.

67 dation experiments demonstrated differential proteolytic digestion, as a function of thermal stabilit

68 In limited proteolytic digestion assays, SR11335 induced resistance

69 on approach achieved the same results as the proteolytic-digestion-based methodology in a much shorte

70 The coat protein monomer is susceptible to proteolytic digestion, but limited proteolysis by small

71 analogue Cibacron Blue and was sensitive to proteolytic digestion by chymotrypsin.

72 ty, we observed that Sec61p is shielded from proteolytic digestion by native, bound ribosomes.

73 a 2.9 S particle, and is highly sensitive to proteolytic digestion by proteinase K; these characteris

74 ts the enzyme and enhances susceptibility to proteolytic digestion by the isolated 20 S proteasome.

75 Pet111p was protected from proteolytic digestion by the mitochondrial inner membran

76 proteins due to their presence of impairing proteolytic digestion, causing liquid chromatography col

77 denaturing PAGE and increased sensitivity to proteolytic digestion compared with wild type SOD1.

78 fied by one equivalent of the inhibitor, and proteolytic digestion coupled with LC-MS identified Cys9

79 we created a set of Sup35NM mutants and used proteolytic digestion coupled with mass spectroscopy to

80 t the susceptibility of membrane proteins to proteolytic digestion during HDX-MS is highly protein-sp

81 for marked resistance of trefoil peptides to proteolytic digestion, enabling them to function in the

82 Proteolytic digestion established the presence of both d

83 In addition, circular dichroism and proteolytic digestion experiments revealed structural di

84 alyses using the yeast two-hybrid system and proteolytic digestion experiments suggest that mu1 and m

85 globulin did not support the hypothesis that proteolytic digestion facilitated by pressure is caused

86 sine cross-link (as determined by exhaustive proteolytic digestion followed by cation exchange chroma

87 formation of nitrotyrosine was confirmed by proteolytic digestion followed by high performance liqui

88 LC-MS based peptide mapping, i.e., proteolytic digestion followed by LC-MS/MS analysis, is

89 xidized proteins were collected off-line for proteolytic digestion followed by LC-MS/MS analysis.

90 g Q7-bound products are completely stable to proteolytic digestion for at least 24 h.

91 ied directly by MALDI-TOFMS, or subjected to proteolytic digestion for protein identification.

92 f electronic protein transfer with nanoscale proteolytic digestion in a capillary platform, enabling

93 uclein filaments, because it is resistant to proteolytic digestion in alpha-synuclein filaments; and

94 a subset of lysosomal membrane proteins from proteolytic digestion in intact cells.

95 This nanoscale reaction system enables rapid proteolytic digestion in seconds instead of hours for a

96 embrane extracts, 1a is fully susceptible to proteolytic digestion in the absence of detergent and th

97 29 was also found to be fully susceptible to proteolytic digestion in the absence of detergent and, t

98 of the LukS polypeptide becomes resistant to proteolytic digestion in the fully assembled Luk pore wh

99 their role in protecting the neurotoxin from proteolytic digestion in the GI tract as well as from ad

100 Complexed Chtr is much less reactive toward proteolytic digestion in the presence of high salt than

101 Fibrils showed varied resistance to proteolytic digestion in vitro by either Proteinase K, p

102 Proteolytic digestion indicated that in G43:Ras61L both

103 The susceptibility of PrP(Sc) to proteolytic digestion induced by branched polyamines in

104 egumes, the simulated gastrointestinal tract proteolytic digestion induced marked changes not only in

105 al-time fluorescent microscopy revealed that proteolytic digestion induces either aggregation of the

106 Proteolytic digestion is a key step in peptide mapping w

107 lysis of polypeptide mixtures resulting from proteolytic digestion is described.

108 Manual proteolytic digestion is usually a labor-intensive proce

109 Their proteolytic digestion leads to a large number of peptide

110 Proteolytic digestion mapping showed that the 54-kDa TEF

111 rtial reduction and alkylation, chemical and proteolytic digestion, mass spectrometry, and amino acid

112 region was investigated by fluorescence and proteolytic digestion methods.

113 In contrast, following proteolytic digestion, MsrA is able to fully reduce one-

114 stable, and neither abnormally sensitive to proteolytic digestion nor prone to aggregation.

115 ructure and dynamics were characterized with proteolytic digestion, nucleotide analogue trapping kine

116 aphy or ion mobility spectrometry (IMS), but proteolytic digestion obliterates the crucial PTM connec

117 les such as phosphopeptides generated by the proteolytic digestion of a large protein, eNOS, phosphor

118 ed simultaneously using a multiplex assay by proteolytic digestion of an ADC, if the sites of conjuga

119 Subsequent peptide-centric analysis, through proteolytic digestion of C9 and liquid chromatography (L

120 ative regulated heavy meromyosin prepared by proteolytic digestion of chicken gizzard myosin with bet

121 ormation on cross-linked peptides derived by proteolytic digestion of cross-linked proteins has been

122 hromatography tandem mass spectrometry after proteolytic digestion of extracted proteins, solid-phase

123 are important in the entry process, and that proteolytic digestion of glycoprotein 1 by endosomal pro

124 Proteolytic digestion of inactivated enzyme, followed by

125 yl-terminal tagged G6PT, we demonstrate that proteolytic digestion of intact microsomes resulted in t

126 Proteolytic digestion of milk proteins had no influence

127 Rapid proteolytic digestion of monomeric, non-DNA-bound ER-DBD

128 Limited proteolytic digestion of mutant G2049E and R2063W protei

129 Proteolytic digestion of MutY using thermolysin was foun

130 However, MAb 7.5G slowed the proteolytic digestion of PA by furin in vitro, suggestin

131 After proteolytic digestion of photolabeled DT-A, derivatized

132 detect protease activity (trypsin) based on proteolytic digestion of protamine, and polyanions (pent

133 ods target signature peptides resulting from proteolytic digestion of proteins of the allergenic ingr

134 The approach involves the proteolytic digestion of proteins prior to the isolation

135 includes seven stages of: (1) extraction and proteolytic digestion of proteins to peptides, (2) seque

136 tilizes mass spectral data produced from the proteolytic digestion of proteins, rather than partial o

137 f peptides and peptide mixtures generated by proteolytic digestion of proteins.

138 ions based on analysis of glycopeptides from proteolytic digestion of recombinant human coronaviruse

139 P scaffolds at early time points, indicating proteolytic digestion of scaffolds.

140 ethod of on-probe solubilization and in situ proteolytic digestion of small, acid-soluble spore prote

141 stigated using immunoelectron microscopy and proteolytic digestion of streptolysin O-permeabilized pa

142 Here we describe a method of proteolytic digestion of surface-exposed proteins to ide

143 HDX-MS relies on successful proteolytic digestion of target proteins under acidic co

144 A comparison of the migration and proteolytic digestion of the 54-kDa TEF-1-related polype

145 It is shown here that proteolytic digestion of the C-loop in beta-cardiac myos

146 Selective proteolytic digestion of the central glycosylated region

147 Proteolytic digestion of the Co3+-PEPCK complex and isol

148 tein complexes often involves solution-phase proteolytic digestion of the complex.

149 after reduction of the putative Schiff base, proteolytic digestion of the enzyme, and isolation of th

150 Limited proteolytic digestion of the full-length protein reveale

151 ification by IP-dUMP, which was confirmed by proteolytic digestion of the modified protein followed b

152 After proteolytic digestion of the platelet proteins, and isol

153 ter removal of the noncovalent cofactors and proteolytic digestion of the protein moiety.

154 Proteolytic digestion of the rafts does not disrupt the

155 In comparison, proteolytic digestion of the reporters prior to N-glycan

156 Following proteolytic digestion of the resulting covalent complex,

157 MAM relies on proteolytic digestion of the sample followed by reversed

158 res of a set of glycopeptides resulting from proteolytic digestion of the well-characterized glycopro

159 Proteolytic digestion of tissues has been utilized to re

160 rhea in humans are due, at least in part, to proteolytic digestion of toxin A and B molecules by a se

161 multiplexed inhibitor beads with subsequent proteolytic digestion of unbound proteins and peptide-ba

162 racterization and conformational analysis by proteolytic digestion of WT and mutated (NMBD deletion o

163 Limited in vitro proteolytic digestions of a biologically active His-MBP

164 Proteolytic digestions of F-actin with subtilisin and tr

165 Proteolytic digestions of purified forms of clavulanate

166 A series of proteolytic digestions of the 1331A/HIV-gp120 complex al

167 Proteolytic digestions of the labeled enzyme and analysi

168 l ribosome has been achieved by carrying out proteolytic digestions of whole 28 S subunits followed b

169 l ribosome has been achieved by carrying out proteolytic digestions of whole 39 S subunits followed b

170 en subjected to electronic lysis followed by proteolytic digestion on a single microfabricated bioele

171 fusion of cells expressing only gB, and the proteolytic digestion pattern of gB in virions changes i

172 te fusion, result in the same changes in the proteolytic digestion pattern of gB, possibly representi

173 by changes in intrinsic Trp fluorescence and proteolytic digestion pattern.

174 ne) triphosphate (AMPPCP), Ca2+, and Mg2+ on proteolytic digestion patterns, interpreted in the light

175 stern method for examining Galphat-GTPgammaS proteolytic digestion patterns.

176 The methods employed included various proteolytic digestions, peptide mapping, partial reducti

177 The use of complementary proteolytic digestion/peptide fragmentation processes al

178 Their repair may involve proteolytic digestion resulting in DNA-peptide cross-lin

179 ence analysis in insoluble elastin following proteolytic digestion reveal the P'1 residues in the car

180 id sequences of four peptides isolated after proteolytic digestion revealed that the enzyme is highly

181 Limited proteolytic digestion showed labeling sites on nonoverla

182 In vivo proteolytic digestion shows that the C-terminus is expos

183 The proteolytic digestion step converts a purified recombina

184 esis products, without heavy reliance on the proteolytic digestion step.

185 ts on conformation-dependent protection from proteolytic digestion suggest that, in the presence of B

186 vering and capping and its susceptibility to proteolytic digestion, suggesting a conformational chang

187 Through the assessment of proteolytic digestion, tandem mass tag (TMT) labeling, o

188 dence of enamel proteome phosphorylation and proteolytic digestion that occurred in vivo during tooth

189 spectrometry, tandem mass spectrometry, and proteolytic digestion, that recombinant HOS3 has a disti

190 As judged by sensitivity to proteolytic digestion, the disease-causing prion protein

191 as labeled using the PhIAT method, and after proteolytic digestion, the labeled peptides were isolate

192 er the intact protein mass or, after on-chip proteolytic digestion, the peptide mass fingerprint and/

193 After proteolytic digestion, the PhIAT-labeled peptides were a

194 Following proteolytic digestion, the plant UMP/CMP kinase was puri

195 PrPSc proteins showed similar resistance to proteolytic digestion, they differed in their glycoform

196 N-terminal domain of SecA is protected from proteolytic digestion through insertion into the membran

197 After proteolytic digestion, TNM-labeled residues were identif

198 tein conjugates are potentially repaired via proteolytic digestion to DNA-peptide conjugates.

199 hylated, and then subjected to a combination proteolytic digestion to obtain a complex peptide mixtur

200 dynamin I that had been subjected to limited proteolytic digestion to remove the PRD.

201 This study presents on-tissue proteolytic digestion using a microwave irradiation and

202 having very few steps and is easy to perform proteolytic digestion utilizing thermally stable pepsin,

203 The amount of CHAs released during proteolytic digestion was in the range 0.33-2.67g/100g.

204 spectrometric analysis (HDX-MS) coupled with proteolytic digestion was used to identify the early sta

205 gested proteins for reprocessing/consecutive proteolytic digestion, we applied chymotrypsin to redige

206 d-phase HPLC and FAB mass spectrometry after proteolytic digestion, we have identified the sites of m

207 presence of redox reagents used in standard proteolytic digestions; when these are accounted for, a

208 By combining proteolytic digestion with peptide mapping and tandem ma

209 P/polypeptide adduct was greatly narrowed by proteolytic digestion with Pronase, confirming that the

210 tly attached to the polynucleotide following proteolytic digestion with trypsin correspond to amino a