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1 harge isoforms differing by as little as 0.1 pI units.
2 both angiogenic and bactericidal; RNase A-1 (pI 10.2) has neither activity.
3 n solution, has a stoichiometry of 1:1 and a pI of 6.0-6.5.
4 160 kDa, a stoichiometry of 1:1:1:1:1, and a pI of 7.4-8.1.
5 n estimated molecular mass of 77.3 kDa and a pI value of 5.66, characteristics consistent with transf
6 s are used as internal standards to assign a pI value to each individually detected mitochondrial eve
7 nce fully developed, it can potentially be a pI-based sample fractionation tool for proteomic analysi
8 ily oxidized in cultured cells, generating a pI 5.8 isoform, but an artificial C106A mutant was not.
9 dged by native gel electrophoresis and has a pI value of 4.55, as found for most of the fungi of beta
10 ll nucleic acid-interacting proteins, have a pI of 7.94 or higher; virtually all these 12,000 protein
11  the Hbb(dminor) polypeptide, resulting in a pI of 7.85 versus 7.13.
12 ic and spectrophotometric titration showed a pI of 4.22 +/- 0.33 and apparent pK values of 6.74 +/- 0
13  and 45 degrees C, respectively and showed a pI value of 4.6.
14 th Mn(2+) shifted the pI of ExoS(E381D) to a pI identical to secreted ExoS.
15 he pI are often observed for proteins with a pI above 7.0 upon phosphorylation, whereas little change
16 ovo set of peptides/proteins, largely with a pI between 5.0 and 8.0 and a molecular mass distribution
17 y electrospray mass spectrometry, and with a pI of 5.0.
18 sing of the C-terminal Abeta peptides with a pI of 5.3 in the boundary between cSer and Asp-His.
19 tion of ErA, resulting in a main peak with a pI of 7.35 and an acidic species minor peak at 7.0, both
20 ittle change is observed for proteins with a pI of approximately 5.0.
21 Zn was mainly associated to proteins of acid pIs.
22 ed adjuvant polyinosinic:polycytidylic acid (pI:C).
23  to polyriboinosinic:polyribocytidylic acid (pI:C), DCs mount a specific integrated stress response d
24 horesis demonstrated that SWP3 has an acidic pI and a molecular mass of <20 kDa.
25  Only the predominant AMACR IA has an acidic pI and contains the previously identified peroxisomal ta
26 pal tissue exposed to SH exhibited an acidic pI shift of VCP.
27                    Despite an overall acidic pI, the asymmetric electrostatic charge profile suggests
28 ass from 50 to 100 kDa and a slightly acidic pI (5.4-6.8).
29  (four) were located in two strongly acidic (pI 4 to 4.9) domains in the distal N- and C-terminal reg
30  dominant B-cell epitopes within the acidic (pI 5.35) ankyrin repeat-containing 200-kDa major immunor
31                 Both azurin (P. aeruginosa) (pI = 5.6) and subunit II (Cu(A) domain) of ba(3)-type cy
32 dies revealed that LAMP2 has a more alkaline pI in Pompe compared with control iPSC-CMs due largely t
33 sociated with dissolved proteins of alkaline pIs in surface seawater, while Zn was mainly associated
34 h a molecular weight of 33.38+/-0.34kDa, and pI of 6.30+/-0.15 was confirmed in samples of SOD extrac
35 eins differ widely in buffering capacity and pI and therefore the same PTMs may give rise to quite di
36 ters such as disorder, context, charges, and pI.
37 f a phosphoprotein (approximately 20 kDa and pI 5.5) was observed.
38 raction revealed a single spot of 34 kDa and pI 8.8.
39  predicted molecular weight of 17.33 kDa and pI of 7.84.
40 ecular masses ranging from 29 to 40 kDa, and pI values from 5.1 to 6.3.
41 itive rate associated with accurate mass and pI measurements is presented to demonstrate the utility
42 e., secretion signal, cysteine residues, and pI).
43          However, biases in protein size and pI resolution, as well as limitations in sample volume,
44 antigen features, such as protein weight and pI, and subcellular localizations of bacterial proteins.
45 of a few proteins with molecular weights and pI values typical of cathepsin D, E and pepsin.
46 used to electrostatically stabilize the AOx (pI 4.3) on the anode operating on direct electrochemistr
47 ynthesized AOx-AuNPs conjugate from the AOx (pI 4.5) protein (zeta, -30mV) implied good stability of
48  but precipitates at pH 7.2, its approximate pI value.
49  novel tetrapeptide scaffold [Ac-Xaa(1)-Arg-(pI)DPhe-Xaa(4)-NH2] is reported.
50 s-Arg-(pI)DPhe-Tic-NH2], and 41 [Ac-Arg-Arg-(pI)DPhe-DNal(2')-NH2] were more potent (EC50 < 73 nM) th
51 e most potent MC3R agonists, 18 [Ac-Arg-Arg-(pI)DPhe-Tic-NH2], 1 [Ac-His-Arg-(pI)DPhe-Tic-NH2], and 4
52 he-Tic-(pNO2)DPhe-NH2, Ac-His-(pCl)DPhe-Arg-(pI)Phe-NH2, and Ac-Arg-(pCl)DPhe-Tic-(pNO2)DPhe-NH2, rev
53 Ac-Arg-Arg-(pI)DPhe-Tic-NH2], 1 [Ac-His-Arg-(pI)DPhe-Tic-NH2], and 41 [Ac-Arg-Arg-(pI)DPhe-DNal(2')-N
54 plate contains a sequentially reversed "Arg-(pI)DPhe" motif with respect to the classical "Phe-Arg" m
55 ultiple isoforms of TIA-1, TIAR, and AUF1 at pI values that spanned nearly 3 pH units.
56 termine pI of mitochondria report an average pI.
57                   In general, learning-based pI prediction methods (such as Cofactor, SVM and Branca)
58         mcfp-5 resembles mcfp-3 in its basic pI and abundant 3,4-dihydroxyphenyl-L-alanine (Dopa; 30
59                     Both proteins are basic (pI approximately 10) and exhibit Gly-rich peptide repeat
60 oint (pI) is particularly attractive because pI is a well-defined parameter and it is orthogonal to h
61 ntested, motivating our efforts to benchmark pI prediction methods.
62 tallized proteins and the difference between pI and reported pH at which they were crystallized.
63                                         Both pI and Mr. of BSA were modified upon glycation reaction.
64 g protein and peptide samples covering broad pI range.
65 roteins into the desalinator was followed by pI fractionation with MJ-CIEF in less than 1 h.
66 ation of biological molecules in solution by pI.
67 molecular mass of 51,114 Da and a calculated pI of 4.8.
68         The standard deviation of calculated pI values for unmodified peptides from the theoretically
69 nificant relationship between the calculated pI of successfully crystallized proteins and the differe
70 ed an unusual enrichment in highly cationic (pI > 9) proteins.
71                RNase A-2, the more cationic (pI 11.0), is both angiogenic and bactericidal; RNase A-1
72                      In the absence of cDCs, pI:C failed to induce Th1 cell commitment and IgG2c prod
73 ructed with axes of protein mass and charge (pI) and converted to density estimates comparable across
74 C/EBPbeta and C/EBPdelta to endogenous CIITA pI and pIV.
75 a and C/EBPdelta, and their binding to CIITA pI and pIV, in correlation with inhibition of IFN-gamma-
76                Selected proteins and colored pI markers were used as model analytes.
77 omponent ampholyte buffers with well-defined pI cutoff values, controlled separation of protein mixtu
78                          Fluorescein-derived pI markers are used as internal standards to assign a pI
79                Previous methods to determine pI of mitochondria report an average pI.
80 most proteins, the experimentally determined pI is very close to that predicted by the databases.
81                               The determined pI's were 6.2 for Mahoney, 6.7 for MEF-1, and 5.8 for Sa
82 ides of similar molecular mass but different pI, suggesting the possibility of posttranslational modi
83 sylated protein forms separated to different pI.
84 xoS analyzed from eukaryotic cells displayed pI heterogeneity and prompted an analysis of this hetero
85  mammals, other properties of Spot 14 (i.e., pI, subcellular localization, transcriptional control an
86  basic residues indeed changed the effective pI of the protein.
87 roducible fractionation of model fluorescent pI markers and proteins is achieved using single membran
88  isoelectric focusing of several fluorescent pI markers and proteins is demonstrated across pH 3.8-7.
89 strating the applicability of the method for pI determination in micropreparative procedures within a
90 rmodynamics for adding and removing HCN from pI under Titan conditions suggests that such dynamics is
91 ermined as negatively charged glycoproteins (pI < 6) with molecular masses between 100 and 300 kDa.
92 e algae identified in the community also had pI distributions similar to 'salt-in' strategists.
93  binding of the anionic phage coat to a high pI target protein.
94 lay-nonspecific binding by the phage to high pI target proteins.
95 noantennary glycans associated with the high-pI fractions, nor were predominantly tri- and tetra-ante
96                                       Higher pI peaks were found to contain N- and C-terminal heavy-c
97 ved interconversion between the dark, higher pI and bright, lower pI GFP populations is tightly contr
98 tylcarboxylic acid, Anc, JRH420-12), Ac-His-(pI)DPhe-Arg-Trp-NH2 (JRH322-18), chimeric AGRP-melanocor
99 unds at all these hMC4R SNPs include Ac-His-(pI)DPhe-Tic-(pNO2)DPhe-NH2, Ac-His-(pCl)DPhe-Tic-(pNO2)D
100 to pt-DNA versus ds-DNA, and a difference in pI for these two complexes, whereas Klentaq does not, su
101 proteins uncovered unexpected differences in pI and/or size of specific proteins thought to be highly
102 rane proteins, and proteins with extremes in pI and MW.
103 variants of monocolonal antibodies (mAbs) in pI range of 7-10.
104 yield of protein that has a broader range in pI, and reducing experimental time compared to conventio
105 erogeneity with five charge forms ranging in pI from 5.1 to 5.9.
106 DJ-1 isoforms, of which the acidic isoforms (pI 5.5 and 5.7) of DJ-1 monomer and the basic isoforms (
107 5.7) of DJ-1 monomer and the basic isoforms (pI 8.0 and 8.4) of SDS-resistant DJ-1 dimer are selectiv
108 he 4-helix bundle has a unique role, and its pI (7.8) is higher than other rod domains.
109 lubility properties, with one exception: Its pI is higher by nearly one pH unit.
110 creasing pHs, especially at pHs close to its pI (pH 4.0), indicating the occurrence of co-precipitati
111 were identified in CIITA promoters I and IV (pI and pIV).
112  exon 3 and are designated as IB (Mw 22 kDa, pI 10.31) and IIB (Mw 31 kDa, pI 9.44).
113 horter variant form of IIA (IIAs, Mw 28 kDa, pI 9.65), which lacks the 5' half of the alternative fif
114 IB (Mw 22 kDa, pI 10.31) and IIB (Mw 31 kDa, pI 9.44).
115 encodes a 288-amino acid protein (Mw 32 kDa, pI 9.6).
116 ly a single 39-kDa band and a single 39-kDa, pI 5.0 spot on one- and two-dimensional immunoblots of B
117 encodes a 382-amino acid protein (Mw 42 kDa, pI 6.07).
118  An immunoreactive protein spot (MW: 44 kDa, pI: 4.5) was microsequenced and the related cDNA was clo
119 trol the assembly of cytochrome c (12.5 kDa, pI 10.5) and azurin (13.9 kDa, pI 5.7) proteins into sep
120 , a protein spot of MW approximately 75 kDa, pI 5.5 was cored from a Coomassie-stained two-dimensiona
121  c (12.5 kDa, pI 10.5) and azurin (13.9 kDa, pI 5.7) proteins into separate 3D DNA nanocages, in a pr
122 kinase, was straightforward due to the large pI shift upon multiple phosphorylation events.
123 tly all recombinant basic proteins (at least pI-1 > or = 6.94) may be purified from E. coli in a sing
124 resses GA-induced expression of a barley low pI alpha-amylase gene (Amy32b).
125 nthesized and used to selectively enrich low pI peptides from complex mixtures for MALDI-MS detection
126 s, not more than one O-glycosylated Ser, low pI and membrane location.
127         We show that enrichment of these low pI peptides allows acidic proteins to be selectively tar
128 f apoptosis protein-binding protein with low pI (Diablo) protein translocates into the cytosol during
129 ibitor of apoptosis-binding protein with low pI (Smac/DIABLO) into the cytoplasm and substantial incr
130 caspases/direct IAP binding protein with low pI from mitochondria.
131 ibitor of apoptosis-binding protein with low pI may be differentially released from the mitochondria,
132 ibitor of apoptosis-binding protein with low pI were released following the addition of TNF-alpha.
133  caspase/direct IAP-binding protein with low pI) and caspase-9 bind, is a promising strategy for inhi
134 caspases/direct IAP-binding protein with low pI), a factor that neutralizes the protective actions of
135 caspases/direct IAP-binding protein with low pI), caspase activation, and neuronal death.
136 f apoptosis protein-binding protein with low pI), caspase-3 activity (but not procaspase-3 cleavage),
137 ibitor of apoptosis-binding protein with low pI); anti-apoptotic: XIAP (X-linked inhibitor of apoptos
138 caspases/direct IAP binding protein with low pI, and apoptosis-inducing factor release), caspase acti
139  tetra-antennary glycans associated with low-pI fractions.
140                                Acidic (lower pI) peaks were found to represent deamidated and sialyat
141 etween the dark, higher pI and bright, lower pI GFP populations is tightly controlled by differential
142 identifying peptides that tend to have lower pI values.
143 wnregulated protein in A3HtrAOE with a mass, pI and MALDI-TOF spectrum consistent with outer membrane
144 ted mitochondrial event, and a mitochondrial pI distribution is determined.
145 le distributions of individual mitochondrial pI, accurate determination of the pI of individual mitoc
146 ses of redox proteins with acidic-to-neutral pI values have been obtained on pure alkanethiol as well
147                       These shift the normal pI of insulin from 5.4 to approximately 7.
148                                     Obtained pI's were generally in good agreement with known data, d
149 proteins show a substantial acidification of pI and require high salt concentrations for cooperative
150 dard, we have undertaken the benchmarking of pI calculation methods.
151 e of IEF markers for internal calibration of pI.
152      We speculate that the directionality of pI's intermolecular and intramolecular =N-H(...)N hydrog
153 ine protein pI followed by immobilization of pI-resolved proteins.
154                                Inhibition of pI-kappaBalpha by BAY 11-7085 resulted in decreased Bcl-
155 onstrated a separation of binary mixtures of pI markers and proteins without applying any external fi
156 may give rise to quite different patterns of pI shifts in different proteins.
157 RPLC-MS data are used to construct a plot of pI vs MW for a protein mixture.
158 Therefore accurate theoretical prediction of pI would expedite such analysis.
159 n molecular weight that possessed a range of pI values were represented by molecular forms of CgA and
160 and reported, and thus literature reports of pI abound.
161  (pI) selection, but in the specification of pI progeny.
162 l fractionation of peptide mixtures based on pI can be accomplished by varying the pH of the aqueous
163 nd throughput for protein profiling based on pI vs MW.
164 regardless of protein characteristics (MW or pI) or abundance.
165             A protein's isoelectric point or pI corresponds to the solution pH at which its net surfa
166 ic point and (2) the introduction of peptide pI is effective in minimizing both false positive and fa
167 on for measurable adsorption and the peptide pI, and proximity of cationic groups to the surface in t
168             Panulirin is a cationic peptide (pI 9.5) composed of 48 amino acid residues (5.3 kDa), wi
169               The K(D)(2-1) increased as |pH-pI| increased, indicating that the hydrophobic effect is
170              It has a low isoelectric point (pI 1.1) and, therefore, tends to be negatively charged a
171 5) and below (pH 2.5) the isoelectric point (pI approximately 5.3).
172 cations (PTMs) on protein isoelectric point (pI) and molecular weight and displays the calculated pat
173 ted by differences in the isoelectric point (pI) and the ion exchange properties of the printed subst
174 accurate mass and peptide isoelectric point (pI) as identification criteria, and represents a change
175                       The isoelectric point (pI) cutoff in these extractions depends on the pH of the
176 luidic platforms for fast isoelectric point (pI) determinations via free-flow electrophoresis with in
177 fe style and a low median isoelectric point (pI) for all predicted proteins, suggesting a 'salt-in' s
178 ng protein with low pH of isoelectric point (pI) from the mitochondria, and the activation of caspase
179 ractionation based on the isoelectric point (pI) is particularly attractive because pI is a well-defi
180 l protein (ORF3), with an isoelectric point (pI) of 10.0 and a calculated molecular mass of 22.8 kDa.
181 tein Data Bank (PDB), the isoelectric point (pI) of a protein has been explored as a useful indirect
182 olecular weight and lower isoelectric point (pI) of Hu-recA1PI than pd-A1PI.
183 ely one pH unit below the isoelectric point (pI) of the recombinant proteins, most of the latter bind
184 uled out by comparing the isoelectric point (pI) values to the adsorption of proteins to lignin surfa
185 mine sCD44 concentration, isoelectric point (pI), and phosphorylation, respectively.
186  such as applied voltage, isoelectric point (pI), bulk pH, and bulk conductivity, on the protein trap
187   A novel continuous-flow isoelectric point (pI)-based sorting technique has been developed for prote
188 estimation of the protein isoelectric point (pI).
189 o charge inversion at its isoelectric point (pI=5.3) but remained anionic.
190 containing proteins with isoelectric points (pI values) higher than the pI of albumin, a second fract
191  ill-resolved peaks with isoelectric points (pI values) in the range 7.4 to 8.5.
192 g compounds with varying isoelectric points (pI) and pK(a) values over a range of aqueous solution pH
193 rved to exhibit distinct isoelectric points (pI) and, thus, distinct formal electrostatic charges.
194  (CIEF-WCID) method, the isoelectric points (pI) of complete intact polioviruses were determined.
195 fractions based on their isoelectric points (pI) without the use of carrier ampholytes.
196 es (i.e., those with low isoelectric points (pI)) by matrix-assisted laser desorption/ionization-mass
197  that likely have unique isoelectric points (pI), which are related to their surface compositions and
198 eawater exhibit alkaline isoelectric points (pIs of 8.10 and 8.37) and also acid Ips (4.82, 5.13, 5.4
199  the difference in their isoelectric points (pIs) after methyl esterification.
200 tigate the chain conformations of polyimine (pI), a polymer identified as one major component of poly
201 s Senseless not in the primary SO precursor (pI) selection, but in the specification of pI progeny.
202 ed peptides from the theoretically predicted pI values was on average 0.21 pH units, which is more ac
203 k at 7.0, both comparing well with predicted pI values based on the sum of protein residue pKa values
204 te to pI values consistent with predictions (pI 7.0 for one deamidation).
205  copies regarding their selection pressures, pI values and tissue expression patterns, suggesting the
206  is expressed from three distinct promoters (pI, pIII, and pIV) in a developmental and cell type-spec
207 tudy the influence of solvent pH and protein pI on the ionization responses of proteins.
208 size polyacrylamide gel to determine protein pI followed by immobilization of pI-resolved proteins.
209  was roughly 5 units higher than the protein pI.
210 olution was 4-5 units lower than the protein pI.
211                       To effect this protein pI separation, chromatofocusing(CF) is employed whereby
212 liquid separation technique in which protein pI is used as the first-dimension separation parameter.
213 relate, at least qualitatively, with protein pI.
214                         Many basic proteins (pI>7) and putative disease biomarkers are not identified
215                  Four novel 17 kDa proteins (pI 6.5-6.8) were recognized in a proteomic screen of lys
216 ot analysis revealed that the representative pI of the 32-kDa sCD44 was 6.96 +/- 0.07 in POAG versus
217 an be optimized to generate highly resolved, pI-based fractions in solution which can be used for suc
218                      The expressed protein's pI value thus becomes an important parameter together wi
219 rboxyl to lysine substitutions, 5K RNase Sa (pI=10.2), have been determined by NMR at 20 degrees C in
220 atable groups in ribonuclease Sa (RNase Sa) (pI=3.5), and a charge-reversed variant with five carboxy
221 ified forms being fractionated into separate pI compartments.
222 that the intrinsic positive charges of SEVI (pI = 10.21) facilitate virion attachment to and fusion w
223 d been secreted by P. aeruginosa also showed pI heterogeneity with five charge forms ranging in pI fr
224                            The enzyme showed pI of 4.1 and a single polypeptide band of 83.1kDa after
225          Several proteins with a significant pI shift between their isoforms in the patient and contr
226 other hand, required the addition of a small pI range (4-6.5) of ampholytes to improve resolution and
227                           Of these, the SOD1 pI 6.0 isoform is oxidatively modified by carbonylation,
228 ration and isolated peptides within specific pI ranges from sample mixtures, where the pI range was s
229 equence analysis of a 67.8 kDa protein spot (pI 5.7) on a Coomassie-stained two-dimensional (2D) gel
230                        A major protein spot (pI of 5.9 and molecular weight of 37 kDa) was seen in LN
231 e the same for both groups of these strains, pI = 3.4.
232                                   While such pI calculation is widely used, it remains largely untest
233 rency in Titan's atmosphere, indicating that pI could be photochemically active and drive chemistry o
234                                          The pI heterogeneity of ExoS was independent of a mass chang
235                                          The pI of the protein, and optimum pH/temperature of enzyme
236                                          The pI vs MW profile obtained from CIEF-RPLC-MS compares fav
237                                          The pI's of Sabin types 1, 2, and 3 viruses were 7.4, 7.2, a
238 s developed to calculate more accurately the pI values of peptides identified from experimental data.
239 idatively modified by carbonylation, and the pI 5.0 isoform is selectively accumulated in AD and PD.
240 ), and Lys (11.3 and 10.6) peptides, and the pI of BSA (4.8) and FN (5.7), were consistent with publi
241 y to the multi-lectin column (M-LAC) and the pI profiles in IEF separation.
242 eins with pI values in the same range as the pI of albumin, and a third fraction containing proteins
243 soelectric point-commonly referred to as the pI-can be defined as the point of singularity in a titra
244                      At a pH value below the pI of the antibody, a nonmonotonic relationship of T(c)
245                                    Below the pI, the protein molecules were completely and permanentl
246 tigate the disputed relationship between the pI of a protein and the pH at which it crystallizes.
247 the early days of solution biochemistry, the pI has been recorded and reported, and thus literature r
248 inylated oligodeoxynucleotide containing the pI or pIV binding sites, and chromatin immunoprecipitati
249     These devices allow one to determine the pI of a biomolecule from a sample mixture with moderatel
250  the improved device, it was applied for the pI fractionation of yeast proteome digest into 18 fracti
251              Thus, cDCs are required for the pI:C-driven Th1 cell fate commitment but have no crucial
252               Moreover, large changes in the pI are often observed for proteins with a pI above 7.0 u
253 acterized by posttranslational change in the pI of sCD44 and hypophosphorylation, which clearly disti
254     These modifications cause changes in the pI of the protein by adding, removing or changing titrat
255  configuration allows seven fractions in the pI range 3-10 to be analyzed by RPLC-MS in 2 h.
256 V light was demonstrated by the shift in the pI value of Bax on two-dimensional gels and confirmed by
257 on of sCD44 resulted in a basic shift in the pI.
258  with PNGase F or neuraminidase narrowed the pI range, indicating variable degrees of glycosylation a
259 alitatively with trends in B except near the pI of amylase, where physical stability was minimal.
260  found that a mobile phase pH value near the pI of the zwitterionic adsorbent surface leads to full r
261 ochondrial pI, accurate determination of the pI of individual mitochondria by the use of internal sta
262 d whey was explained by the proximity of the pI of whey protein (4.9-5.2), where proteins were found
263 proteins are mostly acidic, and based on the pI determined theoretically, apparently all recombinant
264 , and a selected buffer pH, depending on the pI of the recombinant protein.
265 he electrophoretic field required to run the pI-based sorting is generated by the diffusion of buffer
266 cells or phosphorylations that can shift the pI by several pH units.
267 tion of cell lysates with Mn(2+) shifted the pI of ExoS(E381D) to a pI identical to secreted ExoS.
268 Using this adjusted CIEF-WCID technique, the pI of biologically hazardous components like toxins or v
269 oelectric points (pI values) higher than the pI of albumin, a second fraction containing proteins wit
270 ining proteins with pI values lower than the pI of albumin.
271                  It is demonstrated that the pI for expressed intact proteins as generated by CF is a
272 ed at acidic pH, with a maximum close to the pI of actin.
273                      At pH 7.1, close to the pI of the antibody, a decrease of T(c) versus ionic stre
274           In other cases, however, where the pI is observed to be shifted from the expected value, it
275 ic pI ranges from sample mixtures, where the pI range was simply set by the pH values of the buffer s
276 al muscle mitochondria) and to determine the pIs of other biological or nonbiological particles.
277 based program, pIMethylation, to predict the pIs for peptides with and without methyl esterification.
278  through the avidin zone regardless of their pI values.
279      This allowed the determination of their pI via multispectral imaging of protein and pH sensor fl
280  modified insulins, demonstrating that their pI values were shifted in the expected manner.
281 bunits traveled primarily according to their pI and apparently were not associated with other protein
282     Peptide fractionation according to their pI is also widely used in current proteomics sample prep
283 tionating protein samples according to their pI values without using ampholytes.
284 peptides left the focusing gel because their pIs are higher than the upper limit of the immobilized p
285 brary, identifying the two subunits by their pIs and molecular weights.
286  molecular mass of 72.3 kD and a theoretical pI of 8.78.
287 IEF results were consistent with theoretical pIs of methylated peptides calculated by pIMethylation.
288 type cytochrome c oxidase (T. thermophilus) (pI = 6.0) exhibit optimal voltammetric responses on 1:1
289                                        These pI values measured with the developed method were close
290 mutants were also demonstrated to migrate to pI values consistent with predictions (pI 7.0 for one de
291 observed post-translational modifications to pI shifts relative to the unmodified protein of interest
292  More recently, an off-line method that uses pI-based separation on immobilized pH gradients was deve
293 ed VCP expression and an acidic shift in VCP pI, which was inhibited by protein phosphatase 2A treatm
294 analysis of other acidic polypeptides, whose pI< or =4.
295 entified four human brain SOD1 isoforms with pI values of 6.3, 6.0, 5.7, and 5.0, respectively.
296 longs to the class of neutral proteases with pI value of 6.8, optimal proteolytic activity displayed
297 ization, and identification of proteins with pI values greater than 7.
298 , a second fraction containing proteins with pI values in the same range as the pI of albumin, and a
299 nd a third fraction containing proteins with pI values lower than the pI of albumin.
300                               When used with pI-based fractionation as a first dimension, it provides

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