ライフサイエンスコーパス: proteinase K

1 is accessible to proteolytic degradation by proteinase K.

2 n TonB and ExbD, rendering TonB sensitive to proteinase K.

3 cells, BamA is sensitive to externally added proteinase K.

4 obed without pretreatment of the sample with proteinase K.

5 d by enzymatic digestion by both trypsin and proteinase K.

6 tely eliminated by pretreatment of BMEC with proteinase K.

7 xtension curves when cells were treated with proteinase K.

8 permeable chemical cross-linker BS3 and from proteinase K.

9 odified form is insensitive to the action of proteinase K.

10 iminated by polymyxin B but was destroyed by proteinase K.

11 ophobic and more resistant to proteolysis by proteinase K.

12 ochondria, as evidenced by its resistance to proteinase K.

13 erminal tail from proteolytic degradation by proteinase K.

14 incubation at 50 degrees C in the absence of proteinase K.

15 degradation even in the presence of protease proteinase K.

16 bit excellent proteolytic resistance against proteinase K.

17 lysis when intact bacteria were treated with proteinase K.

18 ophores by means of enzymatic digestion with proteinase K.

19 capsulation mitigated enzyme inactivation by proteinase K.

20 ononucleotide coacervate droplets containing proteinase K (2), and proteinosome-adhered pH-resistant

21 Upon incubation with proteinase K, a conspicuous blue shift of the EOT is obs

22 c, expressed in low abundance, and, based on proteinase K accessibility and opsonophagocytosis assays

23 Proteinase K accessibility assays and whole-cell partiti

24 Data obtained using proteinase K accessibility, TX-114 phase partitioning, a

25 developed as a biosensing platform to detect proteinase K, an enzyme which is a readily available mod

26 The DNA was extracted with proteinase K and analyzed by single-strand conformationa

27 e also partially resistant to proteolysis by proteinase K and chymotrypsin.

28 The cytosolic factor was sensitive to proteinase K and destroyed by boiling, suggesting that i

29 roteins, Osp-specific monoclonal antibodies, proteinase K and formaldehyde as reagents, we found that

30 observed following both cyst treatments with proteinase K and performing experiments at extremes of p

31 -HCl buffer, and enzymatic hydrolysis (using proteinase K and protease XIV).

32 mear on a Western blot that was sensitive to proteinase K and resistant to periodate treatment and gl

33 rions, we also analyzed virions treated with proteinase K and samples prepared from mock-infected cel

34 tes was abrogated by treatment with boiling, proteinase K, and geldanamycin, an inhibitor of hsps, su

35 tructure, resistance to limited digestion by proteinase K, and high thermodynamic stability.

36 leaved by non-BoNT proteases (e.g., trypsin, proteinase K, and thermolysin) while obeying Michaelis-M

37 e comparisons between the structures using a proteinase K assay.

38 when DeltabamE mutant cells are treated with proteinase K, BamA is degraded beyond detection.

39 Treatment of cells with proteinase K but not glycolipid inhibitor reduced AAV1 a

40 Their bioactivities were resistant to proteinase K but were destroyed by alkaline hydrolysis a

41 was resistant to heat and to digestion with proteinase K, but was susceptible to alkaline hydrolysis

42 proves the number of identified proteins for proteinase K by 731%.

43 ione breakdown was inactivated by trypsin or proteinase K, by heating (56 degrees C) and freezing (-2

44 affin-embedded tissue processed with xylene, proteinase K, citric acid, and pepsin.

45 Localization of eNOS to a proteinase K-cleavable site on the cytoplasmic face of t

46 Thus, the two proteinase K cleavage fragments of IDE retain the substr

47 Furthermore, the presence of additional proteinase K cleavage sites indicated that deletion to r

48 pore linker of hERG is the target domain for proteinase K cleavage.

49 In the absence of cholesterol, trypsin or proteinase K cleaved cytosolic loop 4, generating a prot

50 Exposure of intact cells to proteinase K cleaved the 270-kDa SprA into several large

51 Prior treatment of the RNA with proteinase K completely abolishes RNA infectivity, sugge

52 g PrP(Sc) types 1 and 2 (sCJDMM1-2), we used proteinase K concentrations designed to hydrolyse all fr

53 duced by DeltapgfS was highly susceptible to proteinase K degradation, in contrast to the high-molecu

54 ent of wild-type cell extracts with RNase or proteinase K demonstrated that the methyl-accepting subs

55 Additional tests on spectra from proteinase-K digest data showed similar performance impr

56 ructures, as visualized by immunoblotting of proteinase K-digested whole-cell preparations.

57 The purification methods included (i) proteinase K digestion (PKD) and heat inactivation; (ii)

58 Synaptic and fine granular proteinase K digestion (PrPres) immunoreactivity is foun

59 f TSE strains retained similar resistance to proteinase K digestion after heating to below or above t

60 olecular mass of fragments following limited proteinase K digestion and by differing ratios of di-, m

61 orientation of the Lep tag was determined by proteinase K digestion and endoglycosidase H (Endo H) cl

62 2/6 and elicit inflammation was sensitive to proteinase K digestion and independent of traditional N-

63 esidues 134-215 of rPrP106 is protected from proteinase K digestion and possesses a solvent-independe

64 seq is a modified protocol that replaces the proteinase K digestion applied in FiT-seq with extended

65 receptor activity, we developed a live cell proteinase K digestion assay that demonstrated altered c

66 Protection of the Ca2+ATPase (SERCA) from proteinase K digestion has been observed following the a

67 c molecules were > 20-fold more sensitive to proteinase K digestion in low ionic strength buffers tha

68 Proteinase K digestion of either transgenic mitochondria

69 Proteinase K digestion of PrP(Sc) leads to a proteolytic

70 modified oligonucleotide resulting from the proteinase K digestion of the vaccinia topoisomerase I-D

71 After soft lysis of VSV with proteinase K digestion of viral capsid and ribonucleopro

72 and Hyper) were subjected to dgPMCAb, their proteinase K digestion profile underwent a dramatic tran

73 Proteinase K digestion revealed conformational differenc

74 Limited proteinase K digestion revealed strain-specific PrP(Sc)

75 y results from using 1500 to 3000 LCM cells, proteinase K digestion was superior for lower cell numbe

76 h SusF, because SusE was less susceptible to proteinase K digestion when SusF was present, and nonden

77 , we examine 2568 peptides generated through proteinase K digestion, a technique that produces a grea

78 in is characterized by partial resistance to proteinase K digestion, affinity for amyloid-specific dy

79 roscopy (FTIR), hydrogen-deuterium exchange, proteinase K digestion, and binding of a conformation-se

80 tact B. burgdorferi cells was insensitive to proteinase K digestion, and indirect immunofluorescence

81 Spx1 was resistant to limited proteinase K digestion, but was unrelated to the express

82 (1-->4)-beta-glucan synthase is sensitive to proteinase K digestion, indicating that part of the cata

83 0 degrees C for 30 min, and was resistant to proteinase K digestion, suggesting involvement of a lipo

84 PC4 tag at the N terminus was protected from proteinase K digestion, whereas an HPC4 tag at the C ter

85 imycin A or inactivated by heat treatment or proteinase K digestion.

86 ture, but at pH 4.0 changes were revealed by proteinase K digestion.

87 ion of rPrP and protects its N terminus from proteinase K digestion.

88 species-independent, and is not affected by proteinase K digestion.

89 hich it acquires a conformation resistant to proteinase K digestion.

90 ar morphology and an increased resistance to proteinase K digestion.

91 PDH with tNOX renders the GAPDH resistant to proteinase K digestion.

92 Dpl was found to be soluble and sensitive to proteinase K digestion.

93 TM domain to assess membrane insertion using proteinase K digestion.

94 f the alpha-synuclein fibrils was studied by proteinase K digestion.

95 positive, acetylated, and more resistant to proteinase K digestion.

96 DNA was extracted from all ganglia by proteinase-K digestion (TG) or digestion by a mild lysis

97 Proteinase-K digestion experiments highlight the HR1 reg

98 to SDS, heat, and urea but were sensitive to proteinase-K digestion.

99 lyzates (LFHs) were generated by trypsin and proteinase K digestions.

100 Molar absorptivities of proteinase K digests at 56 degrees C can be predicted by

101 tivities based on absorbance measurements of proteinase K digests has been developed.

102 Trypsin, papain, and proteinase K do not cleave band 3 at or near K743 in int

103 Treatment with proteinase K eliminates these CTD signals, leaving only

104 f the [14C]GAX-like polymer was resistant to proteinase K, endo-polygalacturonase, and endo-xylanase

105 ores revealed remarkable acceleration in the proteinase K enzymatic hydrolysis of the nanoparticulate

106 The best extraction was obtained with proteinase K (extracting approximately 75% of the total

107 achieved with as few as 100 cells when both proteinase K extraction and pooling are applied.

108 gestion with the robust nonspecific protease proteinase K facilitates the identification of covalent

109 ctive ingredients, we devised a method using proteinase K followed by heating to deactivate proteins

110 section from each specimen was digested with proteinase K followed by nucleic acid extraction and PCR

111 nfected erythrocytes by lysing with heat and proteinase K for 10 min and immediately, thereafter, loa

112 s for improved DNA recovery as compared with proteinase K for forensic, biochemical research, genetic

113 s found that conditions using 3 microg/ml of proteinase K for permeabilization and 90 min hybridizati

114 Exposure to either trypsin or proteinase K gradually decondensed and softened chromoso

115 were accompanied by an altered resistance to Proteinase K, higher sedimentation velocities in gradien

116 an renin yet binds very tightly to the yeast proteinase (K(i)=4 nM).

117 nsing platform to detect the presence of the proteinase K in human wound fluid, highlighting the pote

118 detected after treating Golgi vesicles with proteinase K in the presence of Triton X-100.

119 In contrast, the addition of proteinase K inhibited biofilm formation in all strains

120 oduct, and establish the facility with which proteinase K is able to complete the digestion of the po

121 d showed resistance to low concentrations of proteinase K, it was not overtly detrimental to the flie

122 However, AspN, GluC, chymotrypsin, and proteinase K largely benefited from being paired with tr

123 aining His6-tagged insulysin (His6-IDE) with proteinase K led to the initial cleavage of the His tag

124 The proteinase K LFH <3 kDa and a previously characterized p

125 rting enzyme (ACE)-inhibitory activity, only proteinase K LFH <3 kDa exerted an in vivo antihypertens

126 Pepsin LFH <3 kDa but not proteinase K LFH <3 kDa inhibited ACE-dependent vasocons

127 Most abundant peptides in proteinase K LFH <3 kDa were identified by using an ion

128 l") subtilisin (Pr1C), and three clusters of proteinase K-like class II subtilisins: extracellular su

129 Secreted into the plasma by the liver, the proteinase K-like serine protease PCSK9 binds the low-de

130 her genera revealed that this subdivision of proteinase K-like subtilisins into three subfamilies pre

131 lification method to amplify LCM DNA using a proteinase K lysis procedure coupled with a pooling stra

132 cross the membrane, we used trypsin mapping, proteinase K mapping, and chemical modification methods.

133 the plasma membrane upon reculture following proteinase K-mediated clearance of cell-surface proteins

134 linker and made it no longer susceptible to proteinase K-mediated cleavage.

135 ting the need for the cumbersome spheroplast-proteinase K method for topology determinations.

136 firmed by its susceptibility to digestion by proteinase K only when exosomes were exposed to Triton X

137 ich was not reduced by OMV pretreatment with proteinase K or polymyxin B prior to coincubation with I

138 Digestion with proteinase K or trypsin yields complementary information

139 signal, extracts were treated with RNase A, Proteinase K, or heat.

140 Treatment of target cells with proteases (proteinase K, papain, alpha-chymotrypsin, and trypsin) a

141 Treatment of intact B. burgdorferi with proteinase K partially digested BmpA, consistent with a

142 to proteolytic digestion in vitro by either Proteinase K, pepsin or pancreatin.

143 nd broad specific proteases such as Pronase, proteinase K, pepsin, papain, and subtilisin.

144 atA was resistant to sodium dodecyl sulfate, proteinase K, pepsin, trypsin, chymotrypsin and the neut

145 The microaggregate species were resistant to proteinase K, phosphorylated at serine-129, oxidized, an

146 id form displayed a remarkable resistance to proteinase K (PK) and produced a PK-resistant core ident

147 Treatment of PrP(Sc) with proteinase K (PK) before the analysis did not enhance th

148 lipid-induced PrP conformational change with proteinase K (PK) digestion.

149 Consequently, treatment of PrPSc with proteinase K (PK) generates a large PK-resistant C-termi

150 ind anionic lipids and to gain lipid-induced proteinase K (PK) resistance.

151 ct organisms was not appreciably affected by proteinase K (PK) treatment.

152 could be cleaved by extracellularly applied proteinase K (PK), an N-terminal truncation up to amino

153 Two types of proteinase K (PK)-resistant and self-perpetuating recomb

154 Immunoblotting revealed three proteinase K (PK)-resistant bands in CWD, representing d

155 GSS) is characterized by the accumulation of proteinase K (PK)-resistant prion protein fragments (PrP

156 Although the proteinase K (PK)-resistant prion protein, PrP27-30, was

157 The accumulation of proteinase K (PK)-resistant PrP also occurred with simil

158 ains consistently have the highest levels of proteinase K (PK)-resistant PrP species, followed by ME7

159 cephalopathies (TSE) rely on the presence of proteinase K (PK)-resistant PrP(Sc) (PrP-res) in postmor

160 cells results in 4- to 10-fold reduction in proteinase K (PK)-resistant PrP(Sc), implicating redox i

161 , which is detergent-insoluble and partially proteinase K (PK)-resistant, constitutes the major compo

162 rm passage, the mutant cells stably produced proteinase K (PK)-resistant, insoluble, and aggregated a

163 ed in their glycoform profiles and levels of proteinase K (PK)-sensitive and PK-resistant isoforms.

164 This was true for samples containing both proteinase K (PK)-sensitive and PK-resistant PrP(Sc) and

165 Most importantly, a putative proteinase K (PK)-sensitive form of PrP(Sc) (sPrP(Sc)) i

166 plexes acquires resistance to degradation by Proteinase K (PK).

167 orm into a beta-sheet structure resistant to proteinase K (PK).

168 selectively cleaved by the serine protease, proteinase K (PK).

169 ion, 'cracking', second fixation, (optional) Proteinase K (Pro-K) or sonication treatment, antibody s

170 te fluorescence measurements combined with a proteinase K protection assay, we show that mutants of F

171 Confocal microscopy and/or proteinase K protection assays of RoDH1, RoDH1 mutants,

172 Using proteinase K protection assays, steady state fluorescenc

173 n exhibit a higher resistance to trypsin and proteinase K proteolysis and a lower exposure of hydroph

174 a recently optimized version of the high pH/proteinase K protocol, provided significant integral mem

175 PrP(Sc) resistance to proteinase K (PrP(res)), residual infectivity by mouse b

176 It is suggested that proteinase K removes the proteins needed for specific su

177 Our data suggest that relative proteinase K resistance does not significantly influence

178 vitro, copper dose-dependently enhanced the proteinase K resistance of the prion protein, and this e

179 process, which involves no further change in proteinase K resistance, occurs more rapidly in the Met(

180 human brain display a distinct intermediate proteinase K resistance, suggesting the detection of a c

181 propagated prions differed in conversion and proteinase K-resistance levels in these astrocytes.

182 substitution does not affect the size of the proteinase K resistant core but controls the mode of lat

183 P(sc) (PrP(res)), the presumed infective and proteinase K resistant particle of the scrapie prion.

184 of hyperphosphorylated and abnormally folded proteinase K resistant tau.

185 evels as well as alpha-synuclein aggregates (proteinase K resistant) and A11 oligomers.

186 The PrP(Sc) aggregate is proteinase K resistant, has a mass of 2,000 kDa or more,

187 y, the tNOX-associated muscle GAPDH also was proteinase K resistant.

188 Progressive aggregation of proteinase-K resistant and Ser129-phosphorylated alpha-s

189 ecombinant PrP amyloid fibrils with extended proteinase-K resistant beta-sheet cores and infrared spe

190 ns of clinically sick mice accumulate longer proteinase K-resistant (PrP(res)) fragments of approxima

191 In addition, larger proteinase K-resistant aggregates developed, along with

192 Furthermore, beta-synuclein formed proteinase K-resistant aggregates in dopaminergic neuron

193 hat NPT100-18A decreased the accumulation of proteinase K-resistant alpha-synuclein aggregates in the

194 nd reduced the levels of ubiquitin, tau, and proteinase K-resistant alpha-synuclein aggregates.

195 thies, including progressive accumulation of proteinase K-resistant alpha-synuclein/ubiquitin aggrega

196 T-QuIC product indicated the generation of a proteinase K-resistant and fibrillary alpha-synuclein sp

197 periplasmic domains of TonB and ExbD and the proteinase K-resistant conformation of TonB.

198 is sufficient to convert PrP to the classic proteinase K-resistant conformation.

199 protein (PrP(C)) into a self-replicating and proteinase K-resistant conformer, termed scrapie PrP (Pr

200 ment results in a substantial extension of a proteinase K-resistant core and is accompanied by an inc

201 " Upon annealing, amyloid fibrils acquired a proteinase K-resistant core identical to that found in b

202 sylated recombinant PrP corresponding to the proteinase K-resistant core of PrP(Sc) and found that it

203 trols, exhibit age-dependent accumulation of proteinase K-resistant endogenous alpha-synuclein in sub

204 ed alpha-synuclein species into insolube and proteinase K-resistant fibres, with strongest accumulati

205 host prion protein (PrP-sen) to the abnormal proteinase K-resistant form (PrP-res).

206 gation of cellular prion protein to a weakly proteinase K-resistant form and induces the synthesis of

207 s characterized in part by accumulation of a proteinase K-resistant form of the prion protein, which

208 triatum led to decrease in the levels of the proteinase K-resistant fraction of alpha-synuclein, amel

209 naled by the development of a characteristic proteinase K-resistant fragment generated by cleavage at

210 PrP forms characterized by abnormally short proteinase K-resistant fragments (atypical PrPres) were

211 es, a form characterized by short C-terminal proteinase K-resistant fragments, in a prion strain of s

212 also increased alphaS tetramers and reduced proteinase K-resistant lipid-rich aggregates.

213 ous GrB to insert into and function within a proteinase K-resistant mitochondrial compartment.

214 was dependent on a neuraminidase-sensitive, proteinase K-resistant molecule.

215 ce again resulted in significantly augmented proteinase K-resistant prion protein deposition and acce

216 sition from cellular prion protein (PrPC) to proteinase K-resistant prion protein scrapie (PrPSc) is

217 f PrP(C), leading to increased generation of proteinase K-resistant prion protein.

218 However, detailed analysis revealed that the proteinase K-resistant profile of PrP(Sc) changed in res

219 between the two forms suggest that atypical proteinase K-resistant PrP (PrPres) gave rise to PrP(Sc)

220 the hallmark features of CJD, spongiosis and proteinase K-resistant PrP aggregates, initially develop

221 rotein and not by deposits of aggregated and proteinase K-resistant PrP alone.

222 d shows that tissues containing little or no proteinase K-resistant PrP can be infectious and harbor

223 D and vCJD samples is mostly associated with proteinase K-resistant PrP species, a known signature of

224 when expressed in ScN2a cells nor generated proteinase K-resistant PrP when expressed in yeast.

225 nerates a C-terminal fragment similar to the proteinase K-resistant PrP(Sc) core of 27-30 kDa implica

226 ibited subsequent maturation of fibrils into proteinase K-resistant PrP(Sc)-like conformation (PrP-re

227 spongiform encephalopathy, and formation of proteinase K-resistant PrP(TSE).

228 r data also suggest that IcsA is folded in a proteinase K-resistant state in the periplasm.

229 induced conversion of PrP(C) to the abnormal proteinase K-resistant state, referred to as atypical Pr

230 alpha-Synuclein (alpha-syn; proteinase K-resistant) and ubiquitin aggregates were fo

231 gregated alpha-synuclein within Lewy bodies (proteinase K-resistant).

232 f the cellular prion protein, PrP(C), into a proteinase K-resistant, amyloid-like aggregate, PrP(Sc).

233 Using a bioassay, we identify a proteinase K-resistant, hydrophobic EBI2 ligand activity

234 onverts cellular prion protein (PrP(C)) into Proteinase K-resistant, infectious PrP particles (PrP(TS

235 normal prion protein (PrPC) to an insoluble, proteinase K-resistant, pathogenic isoform (PrPSc).

236 An atypical proteinase K-resistant, transmissible PrP form that rese

237 ExbD D25N supported conversion of TonB to a proteinase-K-resistant form, but not energization of Ton

238 lly formed oligomers to stable, more compact proteinase-K-resistant oligomers as the key step that le

239 istinct digestion patterns are obtained with proteinase K, revealing interconversion of E1 and E2 or

240 pletely blocked by treating the protein with proteinase K, ruling out lipopolysaccharide contaminatio

241 age III when pmf was present, again becoming proteinase K sensitive, but now able to form the pmf-dep

242 of phosphorylated alpha-synuclein that were proteinase K sensitive, detergent insoluble, and formic

243 t extracts suggest this RNA resides within a proteinase K-sensitive complex.

244 The regulation is mediated by a soluble, proteinase K-sensitive factor, released to the circulati

245 hich has been converted from the endogenous, proteinase K-sensitive form.

246 associated with the conversion of the normal proteinase K-sensitive host prion protein (PrP-sen) to t

247 Here we show a linear increase of proteinase K-sensitive PrP isoforms distinct from classi

248 Glycosylated, N-terminally truncated, proteinase K-sensitive PrP-C with apparent molecular mas

249 physiological, presynaptic alpha-synuclein (proteinase K-sensitive) and highly aggregated alpha-synu

250 pathies (TSE) is the conversion of a normal, proteinase K-sensitive, host-encoded protein, PrP-sen, i

251 animals, there was a 2- to 4-log increase of proteinase K-sensitive, light chain immunoglobulin G (Ig

252 t of ExbD mutants and changes in pmf on TonB proteinase K sensitivity in spheroplasts was examined.

253 onfocal immunofluorescence, antibody access, proteinase K sensitivity, and deglycosylation assays.

254 only ALB/B29-34 and ALB/B36-41 had increased proteinase K sensitivity, ubiquitinylation, and increase

255 vant in vivo system to study changes in TonB proteinase K sensitivity.

256 l digestion of recombinant M. smegmatis with proteinase K showed that Rv1698 is surface-accessible.

257 Proteinase K studies demonstrate that BbHtrA is surface

258 A Proteinase K study showed that proteins incorporated wit

259 isin/kexin type 9 (PCSK9) is a member of the proteinase K subfamily of subtilases that reduces the nu

260 ilisin/kexin type 9 (PCSK9), a member of the proteinase K subfamily of subtilases, promotes internali

261 lisin/kexin type 9a (PCSK9), a member of the proteinase K subfamily of subtilases.

262 kexin type 9a, a protein that belongs to the proteinase K subfamily of subtilases.

263 mitochondria, but treatment with alkali and proteinase K suggested that the Delta5 isoform was more

264 e also extremely resistant to proteolysis by proteinase K, suggesting that a common mechanism may acc

265 was largely accessible to exogenously added proteinase K, suggesting that this protease can access t

266 n of P1D6 was abrogated after digestion with proteinase K, suggesting the protein core of MP contribu

267 Two different enzymes (collagenase and proteinase K) that are known to degrade connective tissu

268 After limited proteolysis by proteinase K, the most abundant fragment from brain-deri

269 highly sensitive to proteolytic digestion by proteinase K; these characteristics suggest a structure

270 ilm was selectively degraded by cutinase and proteinase K to form a porous material.

271 In contrast, proteinase K-treated AD homogenates and Sarkosyl-soluble

272 GalAT activities in proteinase K-treated and untreated Golgi vesicles were s

273 ubstrates and/or immunoblot band profiles of proteinase K-treated RT-QuIC reaction products indicated

274 Proteinase K treatment abrogated IL-8 production elicite

275 ucts fail to enter the gel in the absence of proteinase K treatment and are not observed with an acti

276 Proteinase K treatment at early stages of biofilm develo

277 e detection by the two scFv was sensitive to proteinase K treatment but not to periodate treatment, i

278 background uninfected PBMC counts increased; proteinase K treatment demonstrated some benefit in rest

279 ferred motility upon a pagM null mutant, and proteinase K treatment eliminated motility.

280 Proteinase K treatment of B. burgdorferi cells decreased

281 a disappeared in parallel with SpoVAD during proteinase K treatment of germinated spores.

282 lysis of agarose-encapsulated organisms, (b) proteinase K treatment of intact spirochetes, and (c) Tr

283 Proteinase K treatment of intact vesicles indicates that

284 Proteinase K treatment of methanol-fixed lactobacilli el

285 fugation, size-exclusion chromatography, and proteinase K treatment of plant extracts suggest this RN

286 Proteinase K treatment of the HGE agent or rP44 eliminat

287 Proteinase K treatment of the organelles shows that calp

288 resent in the outer membrane, microscopy and proteinase K treatment showed that enolase does not appe

289 The insensitivity of Fe(0) corrosion to proteinase K treatment suggests that electron uptake fro

290 Notably, proteinase K treatment uncoupled electron uptake from bi

291 as a soluble complex that was insensitive to proteinase K treatment, consistent with MIR2911 being st

292 lular release and their accessibility to the proteinase K treatment, demonstrating the direct involve

293 We additionally show that, after proteinase K treatment, Ile-labeled Ure2p fibrils formed

294 ass beads to break open the fungal cells and proteinase K treatment, RNA was extracted routinely from

295 ctable eNOS was cleaved from mitochondria by proteinase K treatment, suggesting eNOS association with

296 secretion of G-CSF was sensitive to heat and proteinase K treatment, yet insensitive to polymyxin B t

297 ent that potentiates gliding is sensitive to proteinase K treatment.

298 ha-p-tosyl-L-lysine chloromethyl ketone) and proteinase K treatment.

299 gents to permeabilize the tissue rather than proteinase K, which can damage the antigens.

300 Unlike trypsin, proteinase K yielded several fragments that differed in