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1 sates ranged from 0.1% (protex 26L) to 3.7% (pronase).
2 tunicamycin, endoglycosidase H, or protease (pronase).
3 s analogs were determined by incubation with Pronase.
4  and CBD cases predigested with the protease pronase.
5 ein precipitation followed by digestion with Pronase.
6  modes after digestion with bead-immobilized Pronase.
7  to hydrolysis with trypsin only and trypsin-pronase.
8 ore and after treatment of intact cells with pronase.
9 calized in the small complex protection from pronase.
10 moved by internal perfusion of the axon with pronase.
11 d after treatment with chondroitinase AC and pronase.
12                     Cells prior treated with pronase (0.5 U/ml) displayed a complete inhibition of in
13             The nonspecific protease mixture pronase also prevented its formation and resulted in the
14 capacities of the PE extract were similar to pronase and higher than the other microbial enzymes.
15                           It is sensitive to pronase and periodate, indicating that it is likely a gl
16                       Ovomucin hydrolyzed by pronase and protex 26L showed molecular weight (Mw) dist
17 urface bound, as shown by its sensitivity to pronase and the staining pattern revealed by in situ amp
18 od, spleen, or lymph nodes were treated with pronase and then used in a three-color FCXM.
19  The transferable factor(s) was resistant to pronase and trypsin digestion, was heat stable at 56 or
20                                              Pronase and Viscozyme improved the extraction of insolub
21 eatment with protein-modifying agents (heat, pronase, and N-bromosuccinimide) and was blocked by prot
22 s in the (rat) brain and TG were digested by pronase, and THs were extracted with a solid-phase extra
23 leased from their complexes by the action of Pronase, but not DNAse, RNAse, or strong salt solutions,
24      The use of unspecific proteases such as Pronase can largely overcome this problem by generating
25                                              Pronase challenge experiments suggested that the reduced
26  activated HSCs in mice, based on retrograde pronase-collagenase perfusion of the liver and subsequen
27 eatly narrowed by proteolytic digestion with Pronase, confirming that the initial spin-trapped radica
28                               Proteolysis by Pronase converted the anisotropic electron paramagnetic
29    A glycopeptide moiety was isolated from a pronase digest of Fap1 and purified by immunoaffinity ch
30 n site was determined by Edman sequencing of pronase-digested Ambn, which gave HPPPLPXQPS, indicating
31              Methylation linkage analysis of Pronase-digested glycopeptides isolated from BSF wild-ty
32 ients by two different isolation techniques; pronase digestion (9 non-asthmatic, 8 asthmatic) and bro
33 patic cells were isolated by collagenase and pronase digestion followed by centrifugal elutriation, a
34             Small glycopeptides generated by Pronase digestion of gp69/64 also inhibited sperm-egg bi
35                                              Pronase digestion of the G248E P450(cam) mutant after co
36             Earlier studies on the effect of Pronase digestion on receptor activity suggest that this
37                           Incorporation of a pronase digestion step prior to the immunoaffinity LC-MS
38 ptide fragments were susceptible to complete Pronase digestion to their constituent amino acids.
39                            Glycopeptides (by Pronase digestion) were separated by anion-exchange chro
40  isopeptide was identified in the exhaustive Pronase digests of native EF-P and recombinant EF-P isol
41 ically extracted with the proteolytic enzyme pronase E (S. griserus).
42 ations were fragmented using incubation with Pronase E and/or formic acid, and in each case a complet
43 roteins, as pretreatment of pneumococci with pronase E but not sodium periodate significantly reduced
44 nces and yield fragmentation profiles across Pronase E concentrations which can readily be used by ot
45                                    Extensive Pronase E digestion of unlabeled Muclin was used to prod
46                                           At Pronase E loadings of 10 mg, the analysis indicated that
47 ate the influence on digestion efficiency of Pronase E loadings, salinity, natural organic matter con
48              The cells are then treated with Pronase E to degrade residual surface-bound material, an
49    Enzymatic digestion of polypeptides using Pronase E, a protease cocktail, proved preferable to com
50                                     Overall, Pronase E-generated peptide standards were a rapid and e
51                            As a pilot study, Pronase E-generated standards from an Abl kinase sensor
52  A one-enzyme hydrolysis was developed using Pronase E.
53 ed by 57% when bacteria were pretreated with pronase E.
54 rated using Alcalase(TM) (CwCA and CaCA) and Pronase-E (CwCP and CaCP) each for 3 and 6 h, and invest
55 ectins did not affect Ib interactions, while pronase effectively prevented Ib binding to the cell sur
56  fast inactivation by the proteolytic enzyme pronase eliminated charge immobilization, while the spec
57 antibody strength assignment, and the use of pronase for crossmatch.
58 t the PE enzyme may be a good alternative to pronase for extraction of melanoidins.
59 oligosialic chains discovered earlier in the Pronase-generated glycopeptide fraction isolated from th
60 Finally, hydrolysates obtained using trypsin-pronase had a greater antioxidant capacity (ORAC) than c
61 wed that PE had a higher protein content and pronase had higher in carbohydrates.
62 ntiporter monensin and the protease cocktail pronase in multiple mutant backgrounds.
63 e incubated in vitro with LPS, flagellin, or pronase-inactivated flagellin in the presence or absence
64                                           In pronase isolated AECs, 15 DNA regions were differentiall
65                     Selective digestion with pronase, NaOH/NaBH(4), heparinase I, or low pH nitrous a
66 ctivity was heat labile and was abolished by pronase or acid-glycine (pH 2.2) treatment but not by li
67  (0.1%, 1 min each) but not by chymotrypsin, Pronase, or papain (0.1%, up to 2 min each).
68 alpha-p-tosyl-L-lysine chloromethyl ketone), pronase, or proteinase K, suggesting that the functional
69     Murine HSCs were isolated by collagenase-pronase-perfusion, and density gradient centrifugation.
70 trypsin or neuraminidase, had no effect, but pronase pretreatment of RBC resulted in a slight increas
71 orseradish peroxidase (HRP) were digested by Pronase, protected by FmocCl, and efficiently separated
72 pecific and broad specific proteases such as Pronase, proteinase K, pepsin, papain, and subtilisin.
73 eatment of mucin with periodate but not with pronase reduced adherence.
74                       The proteolytic enzyme Pronase reduced the uptake of transferrin, suggesting th
75 A regions were identified with no overlap to pronase regions.
76                                              Pronase-resistant fluorescence was detectable in vesicle
77 each HS-glycosaminoglycan region comprised a pronase-resistant peptide separating two HS chains.
78                        2H5 and KM93 bound to pronase-resistant structures, indicating that the mAbs d
79 rotease N), and 2.4% (flavourzyme) to 46.3% (pronase), respectively.
80 Enzymatic hydrolysis of FPI with trypsin and pronase resulted in a hydrolysate that was fractionated
81 lated WT SOD1 with trypsin, chymotrypsin, or Pronase revealed that the first 63 residues of the N ter
82                               However, it is pronase sensitive and dependent on N-linked glycosylatio
83  We observed that P- and E-selectin bound to pronase-sensitive ligands on murine monocytic WEHI-3 cel
84              Prior treatment of B cells with pronase to remove cell-surface Ig or treatment with BCR-
85 ell FCXM, we utilized the proteolytic enzyme pronase to remove Fc receptors from lymphocytes before t
86 xplored a method using a nonspecific enzyme, pronase, to generate small glycopeptides (between two an
87 e-specific N- and O-glycopeptide analysis of Pronase treated glycoproteins with integrated, sequentia
88     A total of 167 T- and B cell FCXMs using pronase-treated and untreated cells were performed.
89                               Utilization of pronase-treated lymphocytes improves both the sensitivit
90 h a very similar EPR spectrum to that of the Pronase-treated MNP/(center dot)SOD, suggesting that the
91  structures resembling straight filaments or Pronase-treated paired helical filaments raises fundamen
92 ptide cleavage by pepsin or by up to 20 h of Pronase treatment altered fiber assembly kinetics, but t
93                               In this study, pronase treatment improved the specificity of B cell FCX
94                                              Pronase treatment inhibited transfection, whereas dilute
95                                              Pronase treatment of RBCs only modestly altered choleste
96               In contrast, prolonged (>20 h) Pronase treatment resulted in cleavage of the triple hel
97                                              Pronase treatment resulted in improved sensitivity of th
98 a-loaded and dried devices were subjected to pronase treatment yielding the alkylated dipeptide hydro
99 rimary granules was significantly reduced by pronase treatment, boiling, high ionic strength, and mag
100                                        After pronase treatment, T and B cell FCXMs of each patient be
101                                        After pronase treatment, the actual channel values of the nega
102                               However, after pronase treatment, the inhibitory activity of both bikun
103 , were extracted with Viscozyme but not with Pronase treatment.
104 d from the cell surface by either trypsin or pronase treatment.
105 chin, and prodelphinidin dimer A compared to Pronase treatment.
106 fibers were not affected by either pepsin or Pronase treatment.
107               Pretreatment of human EGP with pronase, trypsin, 2-ME, or heating did not interfere wit
108  the surface of human erythrocytes included: pronase, trypsin, beta-mercaptoethanol (2-ME), and heati
109  that BBMs do substantially protect CPE from pronase when this toxin is localized in large complex.
110             Glycoproteins were digested with Pronase yielding primarily glycopeptides and amino acids

 
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