ライフサイエンスコーパス: SDS-PAGE

1 SDS-PAGE analyses indicated the formation of hydrolysate

2 SDS-PAGE analysis (loaded without boiling) of the inacti

3 SDS-PAGE analysis showed that salt addition contributes

4 SDS-PAGE and immunoassay analysis with rabbit polyclonal

5 SDS-PAGE and mass spectrometry identified murine chlorid

6 SDS-PAGE and Western blot analyses indicated that covale

7 SDS-PAGE and Western blot analysis of cell lysates at di

8 SDS-PAGE and Western blot techniques were used to identi

9 SDS-PAGE and western blotting revealed greatly reduced n

10 SDS-PAGE electrophoresis qualitatively detected three ma

11 SDS-PAGE gels stained for catecholase activity showed mu

12 SDS-PAGE gels were used to determine abundance of the CO

13 SDS-PAGE in non-reducing and reducing conditions reveale

14 SDS-PAGE of both roe protein concentrates showed protein

15 SDS-PAGE of pure CPC yielded two bands corresponding to

16 SDS-PAGE patterns show distinctive bands for each kind o

17 SDS-PAGE showed that annonacinone inhibited formation of

18 SDS-PAGE showed that collagens extracted with different

19 SDS-PAGE showed that the molecular mass of purified enzy

20 SDS-PAGE showed that the protein bands corresponding to

21 SDS-PAGE showed that the purified protein had molecular

22 SDS-PAGE shows the presence of a well separated protein

23 SDS-PAGE was carried out for all collagens extracted und

24 SDS-PAGE was performed on type I collagen cross-linked i

25 SDS-PAGE, Western blots, bite blots, and immunization vi

26 tyrosine immunoprecipitations followed by 1D SDS-PAGE and mass spectrometry.

27 OF) spectra of fifteen bands separated by 1D SDS-PAGE.

28 The 2D SDS-PAGE separation demonstrated the presence of a few p

29 Large aggregates unable to enter a 4% SDS-PAGE gel were formed at pH 6.5 and 8.5, which became

30 A SDS-PAGE analysis suggested that Dps should be a substra

31 e the astringency of red wines by means of a SDS-PAGE based-method.

32 After SDS-PAGE of the partially purified material, two separat

33 d a single polypeptide band of 83.1kDa after SDS-PAGE.

34 (T.u.) were analyzed by immunoblotting after SDS-PAGE and Urea-PAGE using polyclonal antibodies (PABs

35 Although SDS-PAGE did not show any differences for either the num

36 Samples are then run on an SDS-PAGE gel and isolated bands are submitted for mass s

37 hange affects migration of the protein on an SDS-PAGE gel, and appears to alter secondary structure o

38 We used an SDS-PAGE-based screen to select peptides that dimerize b

39 Two different analysis methods were used: an SDS-PAGE based assay to detect IgG cleavage products and

40 the level of GABA(A)R subunits on analytical SDS-PAGE, and protein microsequencing establishes that t

41 UV absorbance and SDS-PAGE analyses were used to monitor MR progression du

42 d they were also subjected to amino acid and SDS-PAGE analysis.

43 Both peaks contained PGH activity, and SDS-PAGE revealed that fractions containing activity wer

44 Proteomic analysis and SDS-PAGE electrophoresis of the extracted proteome sugge

45 ultrahigh pressure liquid chromatography and SDS-PAGE gels.

46 e high-performance liquid chromatography and SDS-PAGE indicated intra- and intermolecular cross-linki

47 Gel filtration chromatography and SDS-PAGE revealed that the enzyme is monomeric with a mo

48 aration, lectin affinity chromatography, and SDS-PAGE.

49 ial immunopurification, deglycosylation, and SDS-PAGE separation of FPRs is sufficient to identify C-

50 performance liquid chromatography (HPLC) and SDS-PAGE subunit analysis reveal that the first step of

51 aluated through the degree of hydrolysis and SDS-PAGE profiles.

52 abeling, followed by immunoprecipitation and SDS-PAGE, and in vitro transcription, translation and pr

53 protease showed a single band on native and SDS-PAGE with a molecular weight of 24kDa on SDS-PAGE.

54 olecular weight estimated by NATIVE-PAGE and SDS-PAGE electrophoresis was approximately 60 kDa.

55 ent protein band appeared on native-PAGE and SDS-PAGE implying that the mPPO is a monomeric protein w

56 ptdin control peptides in acid-urea-PAGE and SDS-PAGE, providing identification as putative Crps.

57 protein amount, dynamic light scattering and SDS-PAGE profiling, mass spectrometric protein identific

58 rick tests (SPTs), specific IgEs (sIgEs) and SDS-PAGE immunoblotting.

59 roscopy, secondary ion mass spectrometry and SDS-PAGE indicate that Cba. tepidum biogenic S(0) globul

60 ted using a combination of spectroscopic and SDS-PAGE assays.

61 Spectroscopic and SDS-PAGE binding assays of Sin a 2 and Ara h 1 with diff

62 total reflection-FTIR, CD spectroscopy, and SDS-PAGE.

63 between conclusions reached from TOXCAT and SDS-PAGE data for BNIP3 suggests that accurate estimates

64 We show that TOXCAT and SDS-PAGE give complementary and consistent information a

65 ersisted under cell and lysate treatment and SDS-PAGE conditions that are expected to have suppressed

66 gely steryl esters and triacylglycerols, and SDS-PAGE showed the major proteins to be oleosins.

67 btained by electrophoretic technique such as SDS-PAGE.

68 om the sera of patients with diabetes before SDS-PAGE.

69 Biochemical (SDS-PAGE, Size exclusion chromatography and LC-MS/MS) an

70 Analyses by two-dimensional BN/SDS-PAGE revealed that both types of complexes are compo

71 llagen alpha1/alpha2 ratio was determined by SDS PAGE and by qRT-PCR in ex-vivo bone explants.

72 By SDS-PAGE, two forms of NS5A with distinct apparent molec

73 The protein fractions analysed by SDS-PAGE showed similar bands, indicating different solu

74 Supernatants from each step were analysed by SDS-PAGE, ELISA, and Western blots.

75 t, the samples were dialyzed and analyzed by SDS-PAGE and for OA content.

76 for PMN chemotactic activity and analyzed by SDS-PAGE and mass spectrometry (MS) for unique protein i

77 The digests were analyzed by SDS-PAGE and Western blotting, and cleavage products wer

78 nion-exchange chromatography and analyzed by SDS-PAGE, native PAGE, and Western immunoblot analysis.

79 members show multiple bands when analyzed by SDS-PAGE, suggesting that they may be oligomeric.

80 s were noticeably different when analyzed by SDS-PAGE.

81 min and 2 h, the pellicles were analyzed by SDS-PAGE.

82 displaced with FLAG peptide and analyzed by SDS-PAGE.

83 tion time-of-flight mass spectrometry and by SDS-PAGE using biotinylated PGA1 (PGA1-B).

84 as isolated with high purity, as assessed by SDS-PAGE and native-PAGE zymogram, appearing as a single

85 fflux assay; protein content was assessed by SDS-PAGE Western blot.

86 gomers were reduced (-70.5%), as assessed by SDS-PAGE.

87 ysis of AS-48 digestion fragments in bulk by SDS-PAGE, RP-HPLC, and MALDI-TOF proves that the previou

88 n-tumor brain and neural progenitor cells by SDS-PAGE, immunoblot, mass spectrometry and reverse tran

89 s and from CM cells and was characterized by SDS-PAGE, mass spectrometry, and immunoblotting techniqu

90 lyzed the structure of recombinant CLEC3A by SDS-PAGE and immunoblot, glycan analysis, matrix-assiste

91 d 6.64mgg(-1)) were analysed and compared by SDS-PAGE, showing differences in their electrophoretic p

92 ysates with high specificity as confirmed by SDS-PAGE analysis with a phosphoprotein-specific stain a

93 their triple-helical structure, confirmed by SDS-PAGE and FTIR.

94 om insect cells, and purity was confirmed by SDS-PAGE and mass spectrometry.

95 Peptides were detected by SDS-PAGE and GC-MS was used to determine carbohydrate co

96 itional major peptide bands were detected by SDS-PAGE treatments as compared to the solar or freeze d

97 lous migration of the cross-linked enzyme by SDS-PAGE.

98 The subunit molecular mass estimated by SDS-PAGE was 93 kDa for both strains, while the molecula

99 adation during in vitro GID was evaluated by SDS-PAGE and by measuring the nitrogen content of ultraf

100 ethod, Ara h 1 and Ara h 2 were evaluated by SDS-PAGE and sandwich ELISA.

101 d by recombinant techniques and evaluated by SDS-PAGE, size exclusion chromatography, circular dichro

102 Examination by SDS-PAGE followed by protein staining revealed protein p

103 e deglycosylation rate was first examined by SDS-PAGE at the protein level.

104 tiparallel affinity purification followed by SDS-PAGE analysis is more predictive for expression scre

105 NH(2)-terminal I-like ectodomain followed by SDS-PAGE and microsequencing using electrospray (ISI-Q-T

106 uorescent penicillin BOCILLIN FL followed by SDS-PAGE shows that they are active for acylation by sub

107 -specific chemical cross-linkers followed by SDS-PAGE to determine the proximity of the introduced cy

108 ysis of clarified culture fluid fractions by SDS-PAGE and mass spectrometry revealed that the CTD was

109 few dimerizing sequences were identified by SDS-PAGE.

110 A covalently cross-linked dimer isolated by SDS-PAGE and mass analysis showed that dityrosine dimer

111 a molecular mass of approximately 85 kDa by SDS-PAGE, it elutes in fractions corresponding to approx

112 fractions from felodipine treated lenses by SDS-PAGE in conjunction with mass spectrometry and immun

113 nalysis of human postmortem brain lysates by SDS-PAGE and Western blot reveals htt as full-length and

114 Circular dichroism, heat modifiability by SDS-PAGE, Triton X-114 phase partitioning and liposome i

115 Circular dichroism, heat modifiability by SDS-PAGE, Triton X-114 phase partitioning, and liposome

116 degree of LPO purification was monitored by SDS-PAGE and its R(z) (A(412)/A(280)) value.

117 ultimerization were consistently observed by SDS-PAGE, Western blotting, and mass spectrometry.

118 t analysis of whole-cell lysates obtained by SDS-PAGE and stained with an O-PS-specific monoclonal an

119 haseolin-polyphenol complexation obtained by SDS-PAGE on a 10% polyacrylamide gel, it was observed th

120 ntification of the small cleavage product by SDS-PAGE.

121 Analysis of the protein by SDS-PAGE revealed two subunits with molecular masses of

122 orm 1, which migrates as a 61-kDa protein by SDS-PAGE, is expressed in human islets and pancreatic in

123 (1-2 h); investigate SMALP protein purity by SDS-PAGE analysis and estimate protein concentration (4

124 Identification of proteins resolved by SDS-PAGE depends on robust in-gel protein digestion and

125 rporation into receptor subunits resolved by SDS-PAGE, there was etomidate-inhibitable labeling by [(

126 ferent polypeptide profiles were revealed by SDS-PAGE between exposed and nonexposed pollen, but the

127 ds were detected in purified portal rings by SDS-PAGE under nonreducing conditions.

128 natively, analysis of the inactivated RNR by SDS-PAGE without boiling resulted in 33% of RNR migratin

129 Human retinal proteins were separated by SDS-PAGE and 2D gel electrophoresis (2-DE) and sera from

130 After deglycosylation and separation by SDS-PAGE, excised Coomassie Blue-staining bands ( approx

131 nine, immunoprecipitation, and separation by SDS-PAGE.

132 le enzymatic treatments under sonication, by SDS-PAGE, western blot and ELISA, with serum IgE of alle

133 c congenic mice migrated at a higher m.w. by SDS-PAGE compared with B6 Crry, as a result of different

134 A 28 kDa (apparent molecular weight by SDS-PAGE analysis) soybean protein has been isolated by

135 on of USP20 correlates with a characteristic SDS-PAGE mobility shift of the protein, blocks its deubi

136 vector followed by affinity chromatography, SDS-PAGE, and identification of protein bands evident on

137 es, including size exclusion chromatography, SDS-PAGE, mass spectrometry, and cell stimulation follow

138 binatorial peptide ligand libraries (CPLLs), SDS-PAGE, nLC-ESI-MS/MS, and database search, permitted

139 ced by HPP, this processing modified the 1-D SDS-PAGE sarcoplasmic patterns in a direct-dependent man

140 al assays (thioflavin T, circular dichroism, SDS-PAGE, size exclusion chromatography, surface plasmon

141 If second dimension SDS-PAGE followed BNP, the 180-kDa mutant htt was absent

142 he complex was confirmed by second dimension SDS-PAGE, Western blotting, mass spectrometry, and the u

143 A combination of one-dimensional SDS-PAGE and semi-quantitative mass spectrometry identif

144 Two-dimensional SDS-PAGE of the purified active fraction revealed a sing

145 rom the migration pattern on two-dimensional SDS-PAGE, the majority of plasma CL-K1 was found in comp

146 ation and nonreduced/reduced two-dimensional SDS-PAGE, we detected CL-K1 and CL-L1 in disulfide bridg

147 rmation of complexes that were stable during SDS-PAGE.

148 l sulfate-polyacrylamide gel electrophoresis SDS-PAGE-immunoblotting with patient sera and rabbit ser

149 sulfate polyacrylamide gel electrophoresis (SDS PAGE)-LA ICP MS, and, in duplicate, by 2D IEF-PAGE.

150 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analyses of the holo-ATP synthases were used t

151 Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) analysis revealed the localization of phosviti

152 sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) combined with principal component analysis (PC

153 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) fiber typing and one for Western blot protein

154 sulfate polyacrylamide gel electrophoresis (SDS-PAGE) followed by online post-sizing SDS filtration

155 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel containing a copolymerized protein substra

156 sulfate polyacrylamide gel electrophoresis (SDS-PAGE) helped the separation of these misfolded prote

157 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) is a widely used technique for protein separat

158 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) on minigels can be performed rapidly using sim

159 sulfate- polyacrylamide gel electrophoresis (SDS-PAGE) or capillary gel electrophoresis (CGE) toward

160 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) protocol is described.

161 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed two subunits (approximately 53-kDa an

162 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) separation of proteins followed by in-gel tryp

163 w proteins separated by gel electrophoresis (SDS-PAGE) to be detected as peptides by mass spectrometr

164 sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) to investigate the aggregate structures isolat

165 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used during the CE-SDS peak characterizati

166 naturing polyacrylamide gel electrophoresis (SDS-PAGE) was used to separate proteins.

167 sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and enables SDS-PAGE and subsequent immuno-pr

168 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), oxidative damage to amino acids, and changes

169 sulfate polyacrylamide gel electrophoresis (SDS-PAGE), which was eliminated by phosphatase treatment

170 sulphate-polyacrylamide gel electrophoresis (SDS-PAGE).

171 ulphate-polyaccrylamide gel electrophoresis (SDS-PAGE).

172 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).

173 sulphate polyacrylamide gel electrophoresis (SDS-PAGE).

174 sulfate-polyacrylamide gel electrophoresis (SDS-PAGE)/Western analyses, and the presence of biotinyl

175 dodecyl-polyacrylamide gel electrophoresis (SDS-PAGE, the second-D separation) on either a capillary

176 illar proteins using OFFGEL electrophoresis, SDS-PAGE and protein identification by MALDI-TOF MS.

177 The simple approach employing SDS-PAGE and PCA reported in this paper may provide a us

178 gel electrophoresis (SDS-PAGE), and enables SDS-PAGE and subsequent immuno-probing in an automated m

179 ssays carried out included sugar estimation, SDS-PAGE, GPC, color, FT-IR, DSC, thermal stability, sol

180 As expected, SDS-PAGE patterns were species-specific but differences,

181 Seventeen protein bands from SDS-PAGE were analysed and 26 proteins were identified.

182 Moreover, 19 protein bands from SDS-PAGE were analyzed and a total of 45 different prote

183 were identified as type-I collagens by FTIR, SDS-PAGE, and molecular weight distribution analyses.

184 ional changes (surface hydrophobicity, FTIR, SDS-PAGE and thiol content) of gluten in relation to its

185 Furthermore, SDS-PAGE analysis showed high similarity among the prote

186 130-140- and >150-kDa complexes by gradient SDS-PAGE analysis.

187 y two-dimensional isoelectric focusing (IEF)/SDS-PAGE not only revealed different alpha and beta isof

188 IEF/SDS-PAGE examination of irradiated tadpole brain homogen

189 fate polyacrylamide gel electrophoresis (IEF/SDS-PAGE) and fluorescence measurements.

190 and 70 generated products that comigrated in SDS-PAGE with the C1 and C2 forms, respectively, and mut

191 de sequence, a 76-kDa moiety was detected in SDS-PAGE without reducing agent and heat inactivation.

192 d corresponding to the tetramer (152 kDa) in SDS-PAGE, suggesting that the MGAT2 enzyme primarily fun

193 ated form of Gdown1 with altered mobility in SDS-PAGE that appears during mitosis.

194 ew mecA homolog, showed aberrant mobility in SDS-PAGE, structural instability and loss of activity at

195 No fragmentation was observed in SDS-PAGE while transmission electron micrographs showed

196 r O-linked glycans from proteins resolved in SDS-PAGE gels for subsequent analysis by mass spectromet

197 peptide substrates, by gelatin zymography in SDS-PAGE, and by in situ fluorogenic substrate zymograph

198 Likewise, SDS-PAGE of lavage fluid with high PMN levels showed dis

199 Rather, confocal microscopy, SDS-PAGE, and intrinsic fluorescence measurements indica

200 OXPHOS system and comparative 2D blue native/SDS PAGE analyses using isolated mitochondria.

201 h molecular-weight complexes and Blue Native/SDS-PAGE and isoelectric focusing demonstrated that diff

202 on after immunoprecipitation and blue native/SDS-PAGE.

203 Native PAGE, nonreduced SDS-PAGE, size-exclusion column multiangle laser light s

204 Nonreducing SDS-PAGE revealed that EB-localized apparatus proteins s

205 a discrete "jump" in mobility by nonreducing SDS-PAGE, suggesting formation of at most a few final pa

206 esonance energy transfer (FRET), nonreducing SDS-PAGE, and strategic mutation of the Ab hinge region

207 ic enzymes are first resolved in nonreducing SDS-PAGE on a gel without protein substrate.

208 as demonstrated by glycoprotein staining of SDS PAGE gels.

209 Densitometry analysis of SDS-PAGE gels confirmed no size degradation (P>0.05) as

210 Proteomics tools based on image analysis of SDS-PAGE protein gels and protein identification by tand

211 Through a combination of SDS-PAGE, dependence of ellipticity on protein concentra

212 his method has been used as a replacement of SDS-PAGE for purity analysis of adeno-associated virus (

213 The results of SDS-PAGE gel and Western blot indicated that CRANAD-17 w

214 Herein, we describe the use of SDS-PAGE and microprobe Raman spectroscopy to detect and

215 Without the use of SDS-PAGE for separation, the use of protein A enrichment

216 , an immunoassay method for Abeta oligomers, SDS-PAGE separation of stable oligomers, and atomic forc

217 On SDS-PAGE analysis the composition of cortical fiber cell

218 On SDS-PAGE, AML-1 showed an apparent molecular mass of 27

219 SDS-PAGE with a molecular weight of 24kDa on SDS-PAGE.

220 The enzyme preparation when analysed on SDS-PAGE, displayed a single protein band with Mr 33 kDa

221 It migrated anomalously on SDS-PAGE, similar to the phage T7 scaffolding protein.

222 nized by the alphaOEP80(325-337) antibody on SDS-PAGE.

223 conditions than under reducing conditions on SDS-PAGE.

224 d by these fibroblasts was mildly delayed on SDS-PAGE gel, suggesting some overmodification of collag

225 cated shoulder proteins that are detected on SDS-PAGE as faster-migrating shoulder bands designated L

226 In line with the migration shift detected on SDS-PAGE of cell culture collagen, extracts of bone coll

227 iotinylated protein bands were identified on SDS-PAGE gels.

228 t molecular mass of approximately 150 kDa on SDS-PAGE and did not contain Gbeta5 Mass spectrometry an

229 h an apparent molecular weight of 115 kDa on SDS-PAGE gels.

230 sted as a dimer while migrating at 66 kDa on SDS-PAGE.

231 banding patterns from whole-cell lysates on SDS-PAGE gels, by direct staining and/or immunoblotting,

232 ly recognize the ligand-captured material on SDS-PAGE gels.

233 actually TFPIbeta based on (1) migration on SDS-PAGE before and after deglycosylation, (2) the lack

234 revealed the same abnormal chain pattern on SDS-PAGE with an overabundance of a gamma112 cross-linke

235 membranes, ran as intact dimeric proteins on SDS-PAGE, and migrated as an approximately 1100-kDa band

236 Cell lysates were resolved on SDS-PAGE and analyzed by Western blot.

237 myosin super-family members were revealed on SDS-PAGE.

238 ax exhibits a slight molecular mass shift on SDS-PAGE as compared with recombinant Bax, which suggest

239 which resolved to a single 65-kDa species on SDS-PAGE.

240 beled by a fluorescent tag and visualized on SDS-PAGE gel.

241 ion is not sufficient for regular SDS CGE or SDS-PAGE assay.

242 es by high pressure liquid chromatography or SDS-PAGE, nearly 20 modification sites including acetyla

243 Analyses by SEC, blue native PAGE, SDS-PAGE, and dynamic light scattering indicated that th

244 rocessed 12S globulin by 2D blue-native PAGE/SDS-PAGE indicated that the nhx5 nhx6 knockouts showed c

245 ECs) was determined by semiquantitative PCR, SDS-PAGE/Western blotting, and immunofluorescence staini

246 racterized histologically, by real-time PCR, SDS-PAGE, and Western blot.

247 llected and freeze-dried in order to perform SDS-PAGE and immunoblotting tests.

248 were subjected to analysis of total protein, SDS-PAGE and size exclusion chromatography.

249 ish species were estimated by a quantitative SDS-PAGE.

250 Non-reducing SDS-PAGE confirms assembly of the predicted Cys(820)-lin

251 ts expected molecular weight on non-reducing SDS-PAGE gels and coprecipitates with Prm1-TAP, indicati

252 Congo red-positive fibrils, and non-reducing SDS-PAGE of M129C during fibrillation conditions at diff

253 Non-reducing SDS-PAGE shows two bands of about 38kDa exhibiting stron

254 Analyses by non-reducing SDS-PAGE, size exclusion chromatography, and sedimentati

255 ty column, separated by nonreducing-reducing SDS-PAGE, and identified by mass spectrometry.

256 45 kDa in size when analysed under reducing SDS-PAGE.

257 ha modification with 10% fetal bovine serum; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel elec

258 Despite their structural similarity, SDS-PAGE stability assays and collision-induced dissocia

259 romatography coupled with mass spectrometry, SDS-PAGE and immunoassay.

260 5.0109, as documented by mass spectrometry, SDS-PAGE, isoelectric focusing, size-exclusion chromatog

261 also the high sensitivity of silver stained SDS-PAGE.

262 sensitivity is comparable to silver-stained SDS-PAGE.

263 ion, and intensity analysis of heme staining SDS-PAGE.

264 with the laborious sample preparation steps (SDS-PAGE and the subsequent in-gel digestion).

265 uoyant density centrifugation and subsequent SDS-PAGE and proteomics identified them as degenerating

266 In this study, we used Phos-tag SDS-PAGE to determine the cellular level of phospho-FrzZ

267 ly P amounts in cells determined by Phos-tag SDS-PAGE.

268 The SDS-PAGE analyses of cell lysate samples suggest that BS

269 The SDS-PAGE pattern of A. mellifera proteins honey showed t

270 st degree of hydrolysis of HPIs by HT in the SDS-PAGE profiles.

271 ecular weight complexes were observed in the SDS-PAGE results, indicating an efficient conjugation pr

272 eight was approximately 27.5kDa according to SDS-PAGE, shown a single band in zymography.

273 Acetone treatment of cocoa powder prior to SDS-PAGE led to losses of nitrogenous compounds.

274 ric form when cell lysates were subjected to SDS-PAGE under non-reducing conditions.

275 Tricine SDS-PAGE revealed stepwise truncations of the O antigen

276 t neutral pH by high resolution Tris-Tricine SDS-PAGE and matrix-assisted laser desorption ionization

277 hich is directly relevant to the widely-used SDS-PAGE based slab-gel Western blot, while saving sampl

278 Using SDS-PAGE, we found that Rsp profoundly affected cell sur

279 stimated to be approximately 62,000Da, using SDS-PAGE and 57151Da, based on mass spectrometry results

280 ity of in-depth sulfoglycomic analysis using SDS-PAGE resolved proteins.

281 Proteins were studied by using SDS-PAGE and immunoblotting with sera from patients with

282 purity in eluted fractions, determined using SDS-PAGE analysis or similar analytical techniques.

283 Hydrolysis profiles were displayed using SDS-PAGE.

284 its of equal molecular mass estimated, using SDS-PAGE and native-PAGE electrophoresis, to be 86kDa.

285 of contractile proteins in human heart using SDS-PAGE and three detection methods: specific enzymatic

286 e hydrolysis profiles were illustrated using SDS-PAGE.

287 Indeed, using SDS-PAGE, mass spectrometry and western analyses, we sho

288 ed glycation endproducts were measured using SDS-PAGE gels and by ELISA whereas Amadori products were

289 dodecyl beta-D-maltoside and separated using SDS-PAGE.

290 ight, allowing us to separate subunits using SDS-PAGE.

291 he hydrolysis profiles were visualised using SDS-PAGE.

292 ), using protein A enrichment (without using SDS-PAGE) seems to be a good choice for PK studies which

293 scrambled forms is reversed on CE-SDS versus SDS-PAGE.

294 Via SDS-PAGE, most of the mutant c-monomers exhibited increa

295 of -0.5 Pa/s and then further separated via SDS-PAGE in a 25 mm long channel.

296 the influence of HD on BLG molecular weight SDS-PAGE was used.

297 e bound protein is separated from actin with SDS-PAGE and quantitated using densitometry.

298 lue native (BN) electrophorese combined with SDS-PAGE yielded NOX4 to reside in macromolecular comple

299 he analysis using protein A enrichment (with SDS-PAGE) achieved the detection of the drug at a 50-fol

300 n microscopy and protein identification with SDS-PAGE/mass spectrometry.