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1 sates ranged from 0.1% (protex 26L) to 3.7% (pronase).
2 tunicamycin, endoglycosidase H, or protease (pronase).
3 to hydrolysis with trypsin only and trypsin-pronase.
4 ein precipitation followed by digestion with Pronase.
5 modes after digestion with bead-immobilized Pronase.
6 ore and after treatment of intact cells with pronase.
7 calized in the small complex protection from pronase.
8 moved by internal perfusion of the axon with pronase.
9 d after treatment with chondroitinase AC and pronase.
14 urface bound, as shown by its sensitivity to pronase and the staining pattern revealed by in situ amp
16 The transferable factor(s) was resistant to pronase and trypsin digestion, was heat stable at 56 or
18 eatment with protein-modifying agents (heat, pronase, and N-bromosuccinimide) and was blocked by prot
19 s in the (rat) brain and TG were digested by pronase, and THs were extracted with a solid-phase extra
20 leased from their complexes by the action of Pronase, but not DNAse, RNAse, or strong salt solutions,
23 activated HSCs in mice, based on retrograde pronase-collagenase perfusion of the liver and subsequen
24 eatly narrowed by proteolytic digestion with Pronase, confirming that the initial spin-trapped radica
26 A glycopeptide moiety was isolated from a pronase digest of Fap1 and purified by immunoaffinity ch
27 n site was determined by Edman sequencing of pronase-digested Ambn, which gave HPPPLPXQPS, indicating
28 patic cells were isolated by collagenase and pronase digestion followed by centrifugal elutriation, a
35 isopeptide was identified in the exhaustive Pronase digests of native EF-P and recombinant EF-P isol
36 ations were fragmented using incubation with Pronase E and/or formic acid, and in each case a complet
37 roteins, as pretreatment of pneumococci with pronase E but not sodium periodate significantly reduced
38 nces and yield fragmentation profiles across Pronase E concentrations which can readily be used by ot
41 ate the influence on digestion efficiency of Pronase E loadings, salinity, natural organic matter con
43 Enzymatic digestion of polypeptides using Pronase E, a protease cocktail, proved preferable to com
47 ectins did not affect Ib interactions, while pronase effectively prevented Ib binding to the cell sur
48 fast inactivation by the proteolytic enzyme pronase eliminated charge immobilization, while the spec
50 oligosialic chains discovered earlier in the Pronase-generated glycopeptide fraction isolated from th
51 Finally, hydrolysates obtained using trypsin-pronase had a greater antioxidant capacity (ORAC) than c
52 e incubated in vitro with LPS, flagellin, or pronase-inactivated flagellin in the presence or absence
54 ctivity was heat labile and was abolished by pronase or acid-glycine (pH 2.2) treatment but not by li
56 alpha-p-tosyl-L-lysine chloromethyl ketone), pronase, or proteinase K, suggesting that the functional
58 trypsin or neuraminidase, had no effect, but pronase pretreatment of RBC resulted in a slight increas
59 orseradish peroxidase (HRP) were digested by Pronase, protected by FmocCl, and efficiently separated
60 pecific and broad specific proteases such as Pronase, proteinase K, pepsin, papain, and subtilisin.
67 Enzymatic hydrolysis of FPI with trypsin and pronase resulted in a hydrolysate that was fractionated
68 lated WT SOD1 with trypsin, chymotrypsin, or Pronase revealed that the first 63 residues of the N ter
70 We observed that P- and E-selectin bound to pronase-sensitive ligands on murine monocytic WEHI-3 cel
72 ell FCXM, we utilized the proteolytic enzyme pronase to remove Fc receptors from lymphocytes before t
73 xplored a method using a nonspecific enzyme, pronase, to generate small glycopeptides (between two an
74 e-specific N- and O-glycopeptide analysis of Pronase treated glycoproteins with integrated, sequentia
77 h a very similar EPR spectrum to that of the Pronase-treated MNP/(center dot)SOD, suggesting that the
78 structures resembling straight filaments or Pronase-treated paired helical filaments raises fundamen
79 ptide cleavage by pepsin or by up to 20 h of Pronase treatment altered fiber assembly kinetics, but t
85 a-loaded and dried devices were subjected to pronase treatment yielding the alkylated dipeptide hydro
86 rimary granules was significantly reduced by pronase treatment, boiling, high ionic strength, and mag
95 the surface of human erythrocytes included: pronase, trypsin, beta-mercaptoethanol (2-ME), and heati
96 that BBMs do substantially protect CPE from pronase when this toxin is localized in large complex.
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