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1 Sodium dodecyl sulfate polyacrylamide gel electrophoresi
2 were investigated by 2D isoelectric focusing sodium dodecyl sulfate polyacrylamide gel electrophoresi
3 A new method for on-chip sodium dodecyl sulfate polyacrylamide gel electrophoresi
4 y high-performance liquid chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresi
5 oupled plasma mass spectrometry (ICP MS), 1D sodium dodecyl sulfate polyacrylamide gel electrophoresi
6 ionation by centrifugation and separation by sodium dodecyl sulfate polyacrylamide gel electrophoresi
7 tion of the urine by ultracentrifugation and sodium dodecyl sulfate polyacrylamide gel electrophoresi
8 OTC activity and protein levels detected on sodium dodecyl sulfate polyacrylamide gel electrophoresi
9 P-treated chloroplast, which is evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresi
10 iva L.) coleoptile segments were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresi
11 in all monocot and dicot species tested, and sodium dodecyl sulfate polyacrylamide gel electrophoresi
12 rotein, but no significant alteration in the sodium dodecyl sulfate polyacrylamide gel electrophoresi
13 e membrane glycoprotein, band 3 (detected by sodium dodecyl sulfate polyacrylamide gel electrophoresi
14 reduced electrophoretic mobility (shift) in sodium dodecyl sulfate polyacrylamide gel electrophoresi
15 ctively immobilizes all sized proteins after sodium dodecyl sulfate polyacrylamide gel electrophoresi
16 quality controls, a biologic binding assay, sodium dodecyl sulfate polyacrylamide gel electrophoresi
17 se PLB exists primarily as a homopentamer on sodium dodecyl sulfate polyacrylamide gel electrophoresi
18 Centrifugal fractionation coupled with sodium dodecyl sulfate polyacrylamide gel electrophoresi
19 The use of sodium dodecyl sulfate polyacrylamide gel electrophoresi
20 The assay comprises non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresi
21 that have been noted by nonreduced capillary sodium dodecyl sulfate polyacrylamide gel electrophoresi
22 Analysis of the human plaque tissues by sodium dodecyl sulfate polyacrylamide gel electrophoresi
23 purified to homogeneity and characterized by sodium dodecyl sulfate polyacrylamide gel electrophoresi
24 labeled with the probe and analyzed by both sodium dodecyl sulfate polyacrylamide gel electrophoresi
25 ctions from cascaded FF-IEF were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresi
26 n of the purified receptor was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresi
27 Sodium dodecyl sulfate polyacrylamide gel electrophoresi
28 tric focusing (CIEF) with parallel capillary sodium dodecyl sulfate- polyacrylamide gel electrophores
29 tion of myosin heavy chain (MHC) isoforms by sodium dodecyl sulfate--polyacrylamide gel electrophores
30 and analysis of band patterns on nonreducing sodium dodecyl sulfate--polyacrylamide gel electrophores
31 , which appears as a 145 kDa protein band on sodium dodecyl sulfate--polyacrylamide gel electrophores
32 unodetection in leaf extract was realized by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
33 nion-exchange chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresi
34 Careful sodium dodecyl sulfate-polyacrylamide gel electrophoresi
35 Analysis of the mutant lipopolysaccharide by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
36 ration and subjected to either separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
37 ycosylated, as evidenced by migration during sodium dodecyl sulfate-polyacrylamide gel electrophoresi
38 ractions at 144 and 168 kDa, and analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
39 Da band corresponding to the DAT detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
40 lentil lectin chromatography and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresi
41 nd their component proteins were resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
42 re marked by a dramatic shift in mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
43 om a mouse liver homogenate separated by 1-D sodium dodecyl sulfate-polyacrylamide gel electrophoresi
44 cysteine protease (CP) fraction yielding on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
45 Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
46 The results of sodium dodecyl sulfate-polyacrylamide gel electrophoresi
47 oduced by enzymatic cleavage and purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
48 acids in nAChR subunit fragments isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
49 In addition, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
50 recombinant MAPKAPK2, protein separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
51 re-function probe through its application in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
52 f canine rectus muscles were analyzed, using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
53 ion of phosphoproteins both qualitatively by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
54 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
55 P and L-[G-(3)H]allo-isoleucine, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
56 in fibroblast cultures were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
57 (v) An ORF45 protein band was visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
58 rated with a mass of approximately 46 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
59 as a molecular mass of 26 kD as evidenced by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
60 Analysis of the protein composition by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
61 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
62 protein composition, which were confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
63 Examination by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
64 nd VirB9 complexes detectable by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresi
65 ere resolved in a two-dimensional basic-urea/sodium dodecyl sulfate-polyacrylamide gel electrophoresi
66 acis spores, using a combination of standard sodium dodecyl sulfate-polyacrylamide gel electrophoresi
67 and quantified in cell lysates and medium by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
68 Additionally, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
69 tations of protein compositions indicated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
70 r desorption ionization, gel filtration, and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
71 coli cells, migrated as 33 kD proteins upon sodium dodecyl sulfate-polyacrylamide gel electrophoresi
72 ited different electrophoretic mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
73 A sodium dodecyl sulfate-polyacrylamide gel electrophoresi
74 ity-purified GST subunits by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
75 ent molecular mass of 88 kDa was resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
76 VCaB45 migrates anomalously in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
77 s a molecular mass of 29.5 kD as detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
78 tant were isolated and were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
79 Analysis of GIF by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
80 Using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
81 ht of approximately 88,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
82 The purified proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
83 ion kinase, and p130(cas) migrated faster by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
84 assays has been resolved by second-dimension sodium dodecyl sulfate-polyacrylamide gel electrophoresi
85 igh-pressure liquid chromatography analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
86 ced into M. smegmatis on a multicopy vector, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
87 in close agreement with that determined from sodium dodecyl sulfate-polyacrylamide gel electrophoresi
88 in was isolated from the stromal fraction by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
89 dA-T7 forms multimers that are stable during sodium dodecyl sulfate-polyacrylamide gel electrophoresi
90 peptide has a molecular mass of 75.3 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
91 dged by anion exchange chromatography and by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
92 molecular sieve column chromatography and by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
93 g poly(U)-Sepharose, followed by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresi
94 Purified F.IX was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
95 By sodium dodecyl sulfate-polyacrylamide gel electrophoresi
96 tions of H. ducreyi separated by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresi
97 Gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
98 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
99 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
100 ation with 10% fetal bovine serum; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
101 evaluated in this study were processed using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
102 ies of the variant transmembrane proteins in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
103 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
104 in profiles were compared by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
105 ain, as characterized by their mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
106 psin formed homodimers nearly exclusively on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
107 and outer membrane proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
108 ation by proteins that had been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
109 monomer of approximately 85 kDa, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
110 Native and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
111 by examining the fluorescence profile after sodium dodecyl sulfate-polyacrylamide gel electrophoresi
112 Based on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
113 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
114 By using two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
115 Immunoblotting after sodium dodecyl sulfate-polyacrylamide gel electrophoresi
116 solated protein migrated as a single band in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
117 d by affinity gel chromatography followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
118 (3) fragmentation of protein backbones (via sodium dodecyl sulfate-polyacrylamide gel electrophoresi
119 e and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
120 As determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
121 IRS-CAAX migrated more slowly on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
122 eric form of DsrA (28 to 35 kDa) observed in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
123 etal proteins were isolated and separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
124 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
125 e linkages that were revealed by nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresi
126 e as very high-molecular-weight complexes in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
127 exchange chromatography and characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
128 ssociated forms are easily differentiated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
129 By results of sodium dodecyl sulfate-polyacrylamide gel electrophoresi
130 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
131 The factor Xa-ZPI complex is not stable to sodium dodecyl sulfate-polyacrylamide gel electrophoresi
132 Matrix protein synthesis was analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
133 FXIII subunit proteolysis by thrombin using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
134 Collagen was typed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
135 Using one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
136 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
137 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
138 ed with two forms of CK8 after separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
139 , and the labeled fragments were isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
140 actionation of beta cell nuclear extracts by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
141 Immunohistochemical staining and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
142 membrane proteins that had been separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
143 one from a cotton rat) also were compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
144 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
145 In sodium dodecyl sulfate-polyacrylamide gel electrophoresi
146 s purified by continuous-elution preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresi
147 re much smaller than their apparent sizes on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
148 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
149 nt molecular mass of approximately 67 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
150 determined in anti-p85 immunoprecipitates by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
151 has a relative molecular weight of 67,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
152 nd to be similar in size (27 and 27.5 kD) by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
153 Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
154 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
155 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
156 d recombinant QPs3 shows one protein band in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
157 6 and corroborated by evidence acquired from sodium dodecyl sulfate-polyacrylamide gel electrophoresi
158 and smooth colony variants were compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
159 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
160 ed BL/6 mice to egg antigens fractionated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
161 The R1 protein migrated at 70 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
162 e proteinase granzyme B was detectable after sodium dodecyl sulfate-polyacrylamide gel electrophoresi
163 utants were confirmed by using PCR analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
164 d and translated in vitro and analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
165 nomalous migration behavior when analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
166 Cryoelectron microscopic studies and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
167 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
168 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
169 eins (Mr 22,000 and 26,000) were observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
170 t migrated much faster than wild-type LOS in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
171 r (M(r), approximately 50,000), estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
172 expressing TibA or preTibA were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
173 matic tests, whole cell fatty acid analysis, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
174 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
175 ctrophoresis patterns of nasal secretions in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
176 120/sCD4 complex with subsequent analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
177 ed more rapidly than wild-type Ste18p during sodium dodecyl sulfate-polyacrylamide gel electrophoresi
178 264) were clipped into two portions: one for sodium dodecyl sulfate-polyacrylamide gel electrophoresi
179 he patient's clot from recalcified plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
180 of these two transducers, as demonstrated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
181 he density of the silver-stained fraction on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
182 nsoluble and soluble fractions, separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
183 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
184 y 1,300-kDa region containing CSL as seen by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
185 by differential centrifugation, separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
186 However, sodium dodecyl sulfate-polyacrylamide gel electrophoresi
187 orylated in response to SP-A, as resolved by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
188 tivators APAF-1 and cytochrome c as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
189 was measured by scintillation counting after sodium dodecyl sulfate-polyacrylamide gel electrophoresi
190 bunit as detected by mobility retardation on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
191 ded 40- to 55-kDa proteins, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
192 assays, ultraviolet light cross-linking, and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
193 on and sensitive detection of protein during sodium dodecyl sulfate-polyacrylamide gel electrophoresi
194 produces a 40-kDa polypeptide detectable by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
195 tive molecular weight of 39,000, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
196 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
197 35S-methionine labeling and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
198 s and purified to homogeneity by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresi
199 Amino acid composition analysis and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
200 olished expression of CBF1, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
201 antibodies and which comigrated with HA/P in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
202 purified enzyme migrates as a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
203 in digestion of a unique protein isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
204 latelets followed by immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
205 P70) and GroEL (cpn60) using two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
206 d serum albumin levels were determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
207 Comparison by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
208 otease-containing samples into a nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresi
209 a molecular mass of 35 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
210 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
211 arboxymethylated transferrin zymography, and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
212 cted from the size of paranemin (280 kDa) by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
213 and peptides containing 3H were isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
214 ic focusing, and fractions were subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresi
215 e gCIII complex, separated the components by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
216 een shown to decrease the mobility of PLB in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
217 ed a comparison of their protein profiles by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
218 tion on two-dimensional isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresi
219 A modified Laemmli sodium dodecyl sulfate-polyacrylamide gel electrophoresi
220 and from normal corneas were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
221 somes were purified and analyzed by gradient sodium dodecyl sulfate-polyacrylamide gel electrophoresi
222 HeLa cell extracts without heating prior to sodium dodecyl sulfate-polyacrylamide gel electrophoresi
223 A molecular weight shift was observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
224 and cultured lacrimal acini from rabbits by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
225 essed by Southwestern blot analysis in which sodium dodecyl sulfate-polyacrylamide gel electrophoresi
226 fact two proteins, both running at 66 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
227 a fraction which yielded two major bands on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
228 Analysis of the recombinant proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
229 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
230 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
231 In addition, when sodium dodecyl sulfate-polyacrylamide gel electrophoresi
232 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
233 tability, we used a diagonal two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
234 Proteins were separated on a sodium dodecyl sulfate-polyacrylamide gel electrophoresi
235 ion separation of alpha- and beta-tubulin by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
236 ProMMP processing was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
237 Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
238 rotein quantification strategy that involves sodium dodecyl sulfate-polyacrylamide gel electrophoresi
239 in each purified fraction were verified via sodium dodecyl sulfate-polyacrylamide gel electrophoresi
240 yperphosphorylated forms of tau with altered sodium dodecyl sulfate-polyacrylamide gel electrophoresi
241 gically active fractions were resolved using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
242 ains 43895OR and 43895 using one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
243 two carbohydrate-containing components with sodium dodecyl sulfate-polyacrylamide gel electrophoresi
244 ysis using an albumin depletion method (with sodium dodecyl sulfate-polyacrylamide gel electrophoresi
245 d proteins were identified as calmodulins by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
246 alyzed by changes in protein migration using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
247 edia were subjected to gel-based separation (sodium dodecyl sulfate-polyacrylamide gel electrophoresi
248 Zta-associated proteins were isolated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
249 urea-polyacrylamide gel electrophoresis and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
250 739, alter the mobility of Ebola virus NP by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
251 of Cha demonstrated mobility as a trimer on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
252 osylated and accounts for the 58-kDa size by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
253 s His(6)-SQS gave a single band at 42 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
254 ack most extractable coat protein as seen by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
255 The P. ubique enzyme possessed an M(r) on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
256 Samples were resolved using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
257 finity IgG from chronic chagasic sera and on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
258 roteins was quantified by performing tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresi
259 1R and TRIM5alpha proteins exhibited similar sodium dodecyl sulfate-polyacrylamide gel electrophoresi
260 Two-dimensional blue native-sodium dodecyl sulfate-polyacrylamide gel electrophoresi
261 yptic digest of the protein extracted from a sodium dodecyl sulfate-polyacrylamide gel electrophoresi
262 evidence obtained by conventional methods of sodium dodecyl sulfate-polyacrylamide gel electrophoresi
263 nd identified 60 proteins by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
264 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
265 addition, the mobility of gH, gB, and gD in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
266 Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
267 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
268 52 kDa, respectively, based on non-reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresi
269 e proteins were separated by one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
270 ilage, separation of the protein mixtures by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
271 Twelve virion proteins were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
272 atus by negative staining, spectroscopy, and sodium dodecyl sulfate-polyacrylamide gel electrophoresi
273 chain-light chain dimer ("half-antibody") on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
274 rimary Vhs translation product comigrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
275 t with transcriptional data, two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
276 m each step of purification were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
277 proteins prior to on-chip protein sizing by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
278 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
279 as investigated by immobilized trypsin using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
280 determined by separation on two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
281 By using two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresi
282 two predominant bands (31.7 and 26.1 kDa) in sodium dodecyl sulfate-polyacrylamide gel electrophoresi
283 f the extent of cleavage after separation by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
284 VSH-1 capsids or with tails were purified by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
285 We have performed sodium dodecyl sulfate-polyacrylamide gel electrophoresi
286 protein with a molecular mass of 180 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
287 units covalently bound to the synthase using sodium dodecyl sulfate-polyacrylamide gel electrophoresi
288 ta 1- and alpha 3-integrins were assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
289 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
290 GTR was observable as a 49-kDa band on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
291 Modifications were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
292 ue Native polyacrylamide gel electrophoresis/sodium dodecyl sulfate-polyacrylamide gel electrophoresi
293 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
294 appeared to be the same molecular weight on sodium dodecyl sulfate-polyacrylamide gel electrophoresi
295 rrent work, spore extracts were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresi
296 be conveniently coupled to second-dimension sodium dodecyl sulfate-polyacrylamide gel electrophoresi
297 lactosamine-containing LOS by silver-stained sodium dodecyl sulfate-polyacrylamide gel electrophoresi
298 Sodium dodecyl sulfate-polyacrylamide gel electrophoresi
299 were desialylated, reduced, and separated by sodium dodecyl sulfate/polyacrylamide gel electrophoresi
300 mopropanone and analyzed by a combination of sodium dodecyl sulfate/polyacrylamide gel electrophoresi
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