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1 bread using different extracts and conducted SDS-polyacrylamide gel electrophoresis.
2 lting downward mobility shift on nonreducing SDS-polyacrylamide gel electrophoresis.
3 producing an electrophoretic retardation on SDS-polyacrylamide gel electrophoresis.
4 that migrated as a doublet of 120-125 kDa on SDS-polyacrylamide gel electrophoresis.
5 oresis and two peptides of 208 and 63 kDa on SDS-polyacrylamide gel electrophoresis.
6 eduction of disulfides resolved two bands on SDS-polyacrylamide gel electrophoresis.
7 d a faster mobility form of these species on SDS-polyacrylamide gel electrophoresis.
8 ical cross-linking assay in conjunction with SDS-polyacrylamide gel electrophoresis.
9 n human T-cells migrated as a 15-kDa band by SDS-polyacrylamide gel electrophoresis.
10 nd migrates as a single band of 55 kDa after SDS-polyacrylamide gel electrophoresis.
11 e and migrates as a single band at 54 kDa on SDS-polyacrylamide gel electrophoresis.
12 rated at 44 and 48 kDa, respectively, during SDS-polyacrylamide gel electrophoresis.
13 -linked proteins unable to enter gels during SDS-polyacrylamide gel electrophoresis.
14 s of the largest subunit can be separated by SDS-polyacrylamide gel electrophoresis.
15 nce thin-layer chromatographic analysis, and SDS-polyacrylamide gel electrophoresis.
16 parent molecular mass of 31 kDa as judged by SDS-polyacrylamide gel electrophoresis.
17 d with Man-6-P and then quantified following SDS-polyacrylamide gel electrophoresis.
18 lysate by DEAE-cellulose chromatography and SDS-polyacrylamide gel electrophoresis.
19 n alpha/beta doublet of distinct mobility on SDS-polyacrylamide gel electrophoresis.
20 were identified by immunoblotting following SDS-polyacrylamide gel electrophoresis.
21 es with calmodulin-Sepharose and analyzed by SDS-polyacrylamide gel electrophoresis.
22 o(a) was analyzed by immunoprecipitation and SDS-polyacrylamide gel electrophoresis.
23 apparent sizes ranging from 11 to 17 kDa by SDS-polyacrylamide gel electrophoresis.
24 biology, using Western blot detection after SDS-polyacrylamide gel electrophoresis.
25 product migrated as a 105-110-kDa protein on SDS-polyacrylamide gel electrophoresis.
26 e by increased electrophoretic mobility upon SDS-polyacrylamide gel electrophoresis.
27 reduction, migrated as a 56-kDa component on SDS-polyacrylamide gel electrophoresis.
28 mately 260 kDa when separated by nonreducing SDS-polyacrylamide gel electrophoresis.
29 in covalent complex formation as detected by SDS-polyacrylamide gel electrophoresis.
30 presence of additional bands observed during SDS-polyacrylamide gel electrophoresis.
31 tein resulting in an increase in mobility on SDS-polyacrylamide gel electrophoresis.
32 5,000 Da, as determined by a linear gradient SDS-polyacrylamide gel electrophoresis.
33 eling of proteins can be readily detected by SDS-polyacrylamide gel electrophoresis.
34 itative densitometry following separation by SDS-polyacrylamide gel electrophoresis.
35 r mass approximately 43 kDa when analyzed by SDS-polyacrylamide gel electrophoresis.
36 arker; protein compositions were analyzed by SDS-polyacrylamide gel electrophoresis.
37 igrated as an apoA-II monomer by nonreducing SDS-polyacrylamide gel electrophoresis.
38 uring conditions is routinely performed with SDS-polyacrylamide gel electrophoresis.
39 hic techniques and separation of proteins by SDS-polyacrylamide gel electrophoresis.
40 phy, whereas it is 22.5 kDa when examined by SDS-polyacrylamide gel electrophoresis.
41 he downward mobility shift under nonreducing SDS-polyacrylamide gel electrophoresis.
42 dent decrease in mobility of the receptor in SDS-polyacrylamide gel electrophoresis.
43 hotoaffinity analogs, proteases, and tricine-SDS-polyacrylamide gel electrophoresis.
44 e complexes were analyzed by two-dimensional SDS-polyacrylamide gel electrophoresis.
45 Da and a second of 7.6 kDa, as determined by SDS-polyacrylamide gel electrophoresis.
46 ying the alpha2AR by immunoprecipitation and SDS-polyacrylamide gel electrophoresis.
47 ut the protein migrates as a 130-kDa band on SDS-polyacrylamide gel electrophoresis.
48 cysteine with albumin as shown by nonreduced SDS-polyacrylamide gel electrophoresis.
49 dicated by size exclusion chromatography and SDS-polyacrylamide gel electrophoresis.
50 ted forms that exhibit similar mobilities in SDS-polyacrylamide gel electrophoresis.
51 epharose affinity chromatography followed by SDS-polyacrylamide gel electrophoresis.
52 esolved when cell extracts were subjected to SDS-polyacrylamide gel electrophoresis.
53 0 kDa and hENT2 migrates as 50 and 47 kDa on SDS-polyacrylamide gel electrophoresis.
54 both nonreducing and reducing conditions on SDS-polyacrylamide gel electrophoresis.
55 nd their polypeptide composition analyzed by SDS-polyacrylamide gel electrophoresis.
56 ingle radiolabeled band of predicted size on SDS-polyacrylamide gel electrophoresis.
57 rotein followed by MutS immunoblotting after SDS-polyacrylamide gel electrophoresis.
58 ethylurea-soluble proteins were separated by SDS-polyacrylamide gel electrophoresis.
59 P3A4, and the immunoprecipitates were run on SDS-polyacrylamide gel electrophoresis.
60 adducts and localization of fluorescence by SDS-polyacrylamide gel electrophoresis.
61 of the triple helical domain as indicated by SDS-polyacrylamide gel electrophoresis.
62 ated with specific antiserum and analyzed by SDS/polyacrylamide gel electrophoresis.
63 ed the protein components by two-dimensional SDS-polyacrylamide gel electrophoresis (2D SDS-PAGE).
65 Estimates for the Mr of GlvA determined by SDS-polyacrylamide gel electrophoresis (51,000) and elec
68 prenyl phosphate phosphatase was analyzed by SDS-polyacrylamide gel electrophoresis, a major 33-kDa p
69 d to a single intense 80-kDa protein band on SDS-polyacrylamide gel electrophoresis after silver stai
71 mited number of major bands when analyzed by SDS-polyacrylamide gel electrophoresis, among which is a
72 e high performance liquid chromatography and SDS-polyacrylamide gel electrophoresis: an amino-termina
73 d not form oligomeric structures by standard SDS-polyacrylamide gel electrophoresis analysis and sedi
82 iometry that is consistent with quantitative SDS-polyacrylamide gel electrophoresis analysis of the c
86 eriments combined with mobility of Rrn11p in SDS-polyacrylamide gel electrophoresis analysis relative
90 hy and shown by enzyme activity profiles and SDS-polyacrylamide gel electrophoresis analysis to have
91 ltured COS cells and migrates anomalously on SDS-polyacrylamide gel electrophoresis analysis with app
96 nigmatic protein-SDS complexes formed during SDS polyacrylamide gel electrophoresis and brings a new
97 branes, subjected to sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and Western blot
99 .5 and apparent molecular mass of 130 kDa by SDS-polyacrylamide gel electrophoresis and 160 kDa by no
100 ss of 82 kDa according to gel filtration and SDS-polyacrylamide gel electrophoresis and a pH optimum
102 Phd:Doc as assayed by dye binding following SDS-polyacrylamide gel electrophoresis and as determined
103 Therefore, we renatured the enzyme after SDS-polyacrylamide gel electrophoresis and assayed slice
104 1-212 migrates at 27,000 daltons (p27) upon SDS-polyacrylamide gel electrophoresis and at 32,000 dal
105 tion of NHE3V as analyzed by one-dimensional SDS-polyacrylamide gel electrophoresis and autoradiograp
106 with core of Mr = 42,000 was established by SDS-polyacrylamide gel electrophoresis and autoradiograp
107 d inhibition by PMA based on one-dimensional SDS-polyacrylamide gel electrophoresis and autoradiograp
108 t disuccinimidyl suberate and analyzed by 5% SDS-polyacrylamide gel electrophoresis and autoradiograp
109 esponse fashion, as assessed by migration on SDS-polyacrylamide gel electrophoresis and by an increas
111 protein migrated between 150 and 180 kDa in SDS-polyacrylamide gel electrophoresis and could be reso
112 ed as a single polypeptide of 95 kDa mass by SDS-polyacrylamide gel electrophoresis and deacylated ar
113 idomethylated RHL subunits were separated by SDS-polyacrylamide gel electrophoresis and digested in-g
115 teins are indistinguishable when analyzed by SDS-polyacrylamide gel electrophoresis and exhibit penta
116 from the rod outer segments and subjected to SDS-polyacrylamide gel electrophoresis and fluorography
117 ociated p145 exhibited identical mobility by SDS-polyacrylamide gel electrophoresis and identical pat
120 protein migrated as a single 23-kDa band in SDS-polyacrylamide gel electrophoresis and in Western bl
121 agments of apoE3 to A beta in vitro by using SDS-polyacrylamide gel electrophoresis and intrinsic flu
122 grates as a single band of 44,000 daltons on SDS-polyacrylamide gel electrophoresis and is itself a g
123 mes the molecular mass of native R67 DHFR in SDS-polyacrylamide gel electrophoresis and is monomeric
126 a monomeric form of meprin, as determined by SDS-polyacrylamide gel electrophoresis and nondenaturing
127 on a single band observed at about 67 kDa in SDS-polyacrylamide gel electrophoresis and on a single p
128 ; (iii) fractionate the isolated peptides by SDS-polyacrylamide gel electrophoresis and probe the lad
129 ass of 40 kDa was observed, as determined by SDS-polyacrylamide gel electrophoresis and recovery afte
130 d of two polypeptides of 60-66 and 17 kDa by SDS-polyacrylamide gel electrophoresis and retained a na
131 from unreacted enzyme and oligonucleotide by SDS-polyacrylamide gel electrophoresis and subjected to
132 The resultant products were separated by SDS-polyacrylamide gel electrophoresis and subjected to
133 protein was purified further by preparative SDS-polyacrylamide gel electrophoresis and subjected to
135 an alpha2M and plasma CPB dissociated during SDS-polyacrylamide gel electrophoresis and transverse ur
136 point of the A(2) peptide, as determined by SDS-polyacrylamide gel electrophoresis and two-dimension
137 ould be observed by migration differences in SDS-polyacrylamide gel electrophoresis and was evident i
138 CD ran as an approximately 78-kDa protein on SDS-polyacrylamide gel electrophoresis and was found to
139 erial that comigrated with hepatic lipase on SDS-polyacrylamide gel electrophoresis and was immunorea
140 kDa) and two minor bands (42 and 50 kDa) in SDS-polyacrylamide gel electrophoresis and were immunore
141 ied glycoprotein was 80 kDa as determined by SDS-polyacrylamide gel electrophoresis and Western blot
144 , we compared the oligomeric structure (from SDS-polyacrylamide gel electrophoresis) and function (in
145 harose 4B column chromatography, preparative SDS-polyacrylamide gel electrophoresis, and acetone prec
146 of analytical gel filtration chromatography, SDS-polyacrylamide gel electrophoresis, and amino-termin
148 re studied by gel permeation chromatography, SDS-polyacrylamide gel electrophoresis, and fluorescence
150 luted proteins were subjected to preparative SDS-polyacrylamide gel electrophoresis, and protein corr
151 t neutral pH was followed by gel filtration, SDS-polyacrylamide gel electrophoresis, and scanning tra
152 of the forms, Se-P45B, migrates at 45 kDa on SDS-polyacrylamide gel electrophoresis, and the other, S
153 paration, a band of approximately 100 kDa on SDS-polyacrylamide gel electrophoresis, and turnover num
154 elate chromatography followed by preparative SDS-polyacrylamide gel electrophoresis, and utilized for
155 The enzyme migrates anomalously fast in SDS-polyacrylamide gel electrophoresis (approximately 42
159 e NIS is highly glycosylated, it migrates in SDS-polyacrylamide gel electrophoresis as a broad polype
160 ulted in an Epo-Epo species that migrated on SDS-polyacrylamide gel electrophoresis as a narrow band
161 at least two proteins that were detected by SDS-polyacrylamide gel electrophoresis as a single 200-k
162 a kinase activity with the same mobility by SDS-polyacrylamide gel electrophoresis as authentic bovi
163 oblots using the anti-NUC70 antibody and DNA-SDS-polyacrylamide gel electrophoresis assays indicate t
164 ptide in the chloroplast complex was seen in SDS-polyacrylamide gel electrophoresis at a stoichiometr
165 e resistant to denaturation when examined by SDS-polyacrylamide gel electrophoresis at various pH lev
166 do-GD1b, a radiolabeled band was observed by SDS-polyacrylamide gel electrophoresis autoradiography,
167 d to two-dimensional sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis blotted, and the
168 ked to alpha, giving rise to two products on SDS-polyacrylamide gel electrophoresis, both of which we
169 nsferase migrates at approximately 63 kDa by SDS-polyacrylamide gel electrophoresis but elutes from t
170 ha-Fc ran as a monomer of 60 kDa on reducing SDS-polyacrylamide gel electrophoresis but formed a trim
171 coli migrates as a 160-kilodalton protein in SDS-polyacrylamide gel electrophoresis but has a molecul
172 disulfide bond formation was assessed after SDS-polyacrylamide gel electrophoresis by staining with
173 were substituted by serines, is monomeric on SDS-polyacrylamide gel electrophoresis, can be phosphory
174 olated from each strain and characterized by SDS-polyacrylamide gel electrophoresis, carbohydrate, an
175 Evidence for this hypothesis has come from SDS-polyacrylamide gel electrophoresis, coimmunoprecipit
176 and after limited tryptic proteolysis using SDS-polyacrylamide gel electrophoresis containing 6 M ur
177 near homogeneity; a single band at 25 kDa on SDS-polyacrylamide gel electrophoresis correlated well w
178 major protein band of approximately50 kDa on SDS-polyacrylamide gel electrophoresis correlated with G
179 f heterologously produced Isf (determined by SDS-polyacrylamide gel electrophoresis) corresponded to
180 equentially cross-linked to produce bands on SDS-polyacrylamide gel electrophoresis corresponding in
182 hile causing retardation of its migration on SDS-polyacrylamide gel electrophoresis, decreased ErbB-2
183 te +/- dog pancreatic microsomes followed by SDS-polyacrylamide gel electrophoresis defined the prese
184 alytical ultracentrifugation and nonreducing SDS-polyacrylamide gel electrophoresis demonstrate that
187 rbonate extraction, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis/fluorography.
188 nd peptides containing (3)H were purified by SDS-polyacrylamide gel electrophoresis followed by rever
189 y UG-affinity chromatography and analysis by SDS-polyacrylamide gel electrophoresis followed by silve
190 d paxillin also exhibit reduced migration on SDS-polyacrylamide gel electrophoresis following PMA tre
191 an ARE sequences to beta ARB was revealed by SDS-polyacrylamide gel electrophoresis following UV-cata
192 xcellent accord with 31,000, as estimated by SDS-polyacrylamide gel electrophoresis for purified bovi
195 ists in two forms when visualized by reduced SDS-polyacrylamide gel electrophoresis: (i) intact EC-SO
197 Comparison of their subunit compositions by SDS-polyacrylamide gel electrophoresis indicated that th
198 ut 47.5 kDa on both reducing and nonreducing SDS-polyacrylamide gel electrophoresis, indicating a mon
199 oss-linked products were immunoblotted after SDS-polyacrylamide gel electrophoresis, indistinguishabl
201 PITP, which migrates as a 36-kDa protein in SDS-polyacrylamide gel electrophoresis, is cleaved rapid
202 This was assessed by gel chromatography, SDS-polyacrylamide gel electrophoresis, isoelectric focu
204 molecular weight of approximately 34,000 on SDS-polyacrylamide gel electrophoresis; it is an intrins
205 d a rapid purification procedure followed by SDS- polyacrylamide gel electrophoresis may provide a us
206 ciently converted to a new species that upon SDS-polyacrylamide gel electrophoresis migrated between
208 Purified yapsin 2 migrated diffusely in SDS-polyacrylamide gel electrophoresis (molecular mass a
210 alpain and tryptic cleavage, two-dimensional SDS-polyacrylamide gel electrophoresis, N-terminal seque
213 20 or p22 ICE as determined by band shift on SDS-polyacrylamide gel electrophoresis of the biotinylat
214 e-sensitive protein (45 kDa) was observed by SDS-polyacrylamide gel electrophoresis of the inner memb
215 Subsequent anion-exchange chromatography and SDS-polyacrylamide gel electrophoresis of the microcysti
217 ido-Q-labeled SdhC obtained from preparative SDS-polyacrylamide gel electrophoresis on labeled reduct
218 ould not be segregated from Tg protein by 5% SDS-polyacrylamide gel electrophoresis or by immunopreci
219 ins were either directly resolved using urea/SDS-polyacrylamide gel electrophoresis or first immunopr
220 ly modify either their migration patterns on SDS-polyacrylamide gel electrophoresis or their overall
221 t focusing (TGF) and sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) in a PDMS
222 tive, and label-free sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) method fo
223 to 2-dimensional (2D) sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), transfer
224 neous protein preparation, evidenced by both SDS-polyacrylamide gel electrophoresis (PAGE) and agaros
225 I produced a single monomeric 37-kDa band on SDS-polyacrylamide gel electrophoresis (PAGE) and two di
226 B (wt-PLB), which is primarily a pentamer on SDS-polyacrylamide gel electrophoresis (PAGE) at 25 degr
229 size-exclusion chromatography as well as by SDS-polyacrylamide gel electrophoresis (PAGE), and compa
232 purification step consisting of preparative SDS-polyacrylamide gel electrophoresis, partial peptide
234 y (DY), and 263K TSE strains yielded similar SDS-polyacrylamide gel electrophoresis profiles prior to
235 her with high pressure liquid chromatography/SDS-polyacrylamide gel electrophoresis purification tech
236 reconstitution of catalytic activity from a SDS-polyacrylamide gel electrophoresis purified protein.
237 l-1,4-benzoquinone ([3H]azido-Q) followed by SDS-polyacrylamide gel electrophoresis, radioactivity is
238 nstrated a 63-kDa protein (latent enzyme) on SDS-polyacrylamide gel electrophoresis rather than the a
239 hibited similar molecular mass of 130 kDa on SDS-polyacrylamide gel electrophoresis, recognition by a
240 s of pRb, the migration pattern of which, on SDS-polyacrylamide gel electrophoresis, resembles variou
241 uent monomers showed a decreased mobility on SDS-polyacrylamide gel electrophoresis resulting from an
242 Metabolic labeling, immunoprecipitation, and SDS-polyacrylamide gel electrophoresis reveal that pro-B
243 Analysis of the most purified fraction by SDS-polyacrylamide gel electrophoresis revealed a multip
244 g of this protected fragment and analysis by SDS-polyacrylamide gel electrophoresis revealed a protei
245 ingle protein peak on reverse-phase HPLC and SDS-polyacrylamide gel electrophoresis revealed a single
246 high performance liquid chromatography, and SDS-polyacrylamide gel electrophoresis revealed that sub
247 light inhibition could not be reversed, and SDS-polyacrylamide gel electrophoresis revealed, in addi
248 nfirmed by separation of tryptic peptides in SDS-polyacrylamide gel electrophoresis revealing a singl
249 body to one of the constituents, followed by SDS polyacrylamide gel electrophoresis (SDS-PAGE) and We
250 nents of the regulatory complex separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) or two
251 onine and used to probe membranes containing SDS-polyacrylamide gel electrophoresis separated RC subu
253 from different types of bovine cartilage by SDS-polyacrylamide gel electrophoresis showed a prominen
258 ntation of the enzyme by trypsin followed by SDS-polyacrylamide gel electrophoresis showed that omepr
259 olecular weight aggregates under nonreducing SDS-polyacrylamide gel electrophoresis, suggesting the f
260 Of particular interest is the finding by SDS-polyacrylamide gel electrophoresis that BH4-free eNO
261 a conspicuous silver-stained protein band on SDS-polyacrylamide gel electrophoresis that coincided wi
262 contain a calpastatin protein of 145 kDa on SDS-polyacrylamide gel electrophoresis that comigrates w
263 characterized as a diffuse band of 55 kDa on SDS-polyacrylamide gel electrophoresis that is converted
264 h a protein with an apparent Mr of 24,000 by SDS-polyacrylamide gel electrophoresis that was highly e
265 ed predominantly of a M(r) 51,000 band after SDS-polyacrylamide gel electrophoresis that was photoaff
272 finity chromatography column and analyzed by SDS-polyacrylamide gel electrophoresis, the major protei
273 in mobility of auto-ADP-ribosylated ART5 by SDS-polyacrylamide gel electrophoresis, the modification
274 ing to trimers and hexamers as determined by SDS--polyacrylamide gel electrophoresis--the trimer band
275 ) as judged by a reduction of apparent Mr on SDS-polyacrylamide gel electrophoresis; this oxidized fo
276 r, methyl arachidonyl fluorophosphonate, and SDS-polyacrylamide gel electrophoresis to provide eviden
277 artially purified receptors were resolved on SDS-polyacrylamide gel electrophoresis, transferred to a
278 inant Escherichia coli clone, exhibited (via SDS-polyacrylamide gel electrophoresis) two enzymaticall
280 erved with serum exposure by one-dimensional SDS-polyacrylamide gel electrophoresis, two-dimensional
282 ng the activated and nonactivated enzymes on SDS-polyacrylamide gel electrophoresis under nonreducing
283 raldehyde, ribose, and galactose followed by SDS-polyacrylamide gel electrophoresis under reducing co
284 ent molecular mass of 90 kDa as estimated by SDS-polyacrylamide gel electrophoresis under reducing co
285 tly linked multimers that were stable during SDS-polyacrylamide gel electrophoresis using reducing co
287 he growth factor, purified to homogeneity by SDS-polyacrylamide gel electrophoresis, was identified a
288 ing high resolution isoelectric focusing and SDS-polyacrylamide gel electrophoresis, we confirm that
289 papain digestion and analyzed by nonreducing SDS-polyacrylamide gel electrophoresis were dimeric.
291 protein was composed of three major bands on SDS-polyacrylamide gel electrophoresis which comigrated
292 tion on a glycerol gradient, I labeling, and SDS-polyacrylamide gel electrophoresis. which demonstrat
293 king and analysis by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis with different c
294 e purified enzyme exhibited a single band on SDS-polyacrylamide gel electrophoresis with a subunit ma
295 omatography and migrated as a single band on SDS-polyacrylamide gel electrophoresis with a subunit mo
296 ive intermediate is formed which migrates on SDS-polyacrylamide gel electrophoresis with an molecular
297 cells and recombinant ps20 both resolved on SDS-polyacrylamide gel electrophoresis with apparent mol
300 etected using both reducing and non-reducing SDS-polyacrylamide gel electrophoresis with Western blot
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