ライフサイエンスコーパス: proteinase K

1 erminal tail from 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 ochondria, as evidenced by its resistance to proteinase K.

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

13 after digestion of the scleral samples with proteinase K.

14 degradation even in the presence of protease proteinase K.

15 bit excellent proteolytic resistance against proteinase K.

16 lysis when intact bacteria were treated with proteinase K.

17 ophores by means of enzymatic digestion with proteinase K.

18 capsulation mitigated enzyme inactivation by proteinase K.

19 ophobic and more resistant to proteolysis by proteinase K.

20 is accessible to proteolytic degradation by proteinase K.

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

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

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

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

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

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

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

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

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

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

33 y cells and hyaluran, they were treated with proteinase K and tested by a single or fully nested PCR

34 ng antigens were resistant to treatment with proteinase K and to boiling for 1 h, but were susceptibl

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

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

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

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

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

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

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

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

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

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

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

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

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

52 cleavage of G520L because cells treated with proteinase K could not fuse upon temperature increase bu

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 erized by a markedly increased resistance to proteinase K digestion and a fibrillar morphology (i.e.,

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

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

63 2/6 and elicit inflammation was sensitive to proteinase K digestion and independent of traditional N-

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

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 Limited proteinase K digestion of baculovirus-expressed lambda2

69 Proteinase K digestion of either transgenic mitochondria

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

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

72 Proteinase K digestion of total microsomes consistently

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

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

75 Proteinase K digestion revealed conformational differenc

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

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

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

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

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

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

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

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

84 (1-->4)-beta-glucan synthase is sensitive to proteinase K digestion, indicating that part of the cata

85 0 degrees C for 30 min, and was resistant to proteinase K digestion, suggesting involvement of a lipo

86 After proteinase K digestion, the oligomers retain an intact c

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

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

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

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

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

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

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

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

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

96 smically oriented as shown by sensitivity to proteinase K digestion.

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

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

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

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

101 Proteinase-K digestion experiments highlight the HR1 reg

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

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

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

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

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

107 ase activity was cell associated, reduced by proteinase K, eliminated by boiling, and independent of

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

141 Digestion with proteinase K or trypsin yields complementary information

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

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

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

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

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

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

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

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

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

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

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

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

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

155 s treated with M. penetrans lipid extract of proteinase K (PK)-digested LAMPs.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

172 A proteinase K protection assay revealed a 36-kDa fragment

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

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

175 Using proteinase K protection assays, steady state fluorescenc

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

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

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

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

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

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

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

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

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

185 of hyperphosphorylated and abnormally folded proteinase K resistant tau.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

256 ta1-2 dimer showed that multiple trypsin and proteinase K sites in the A helices of the beta2 and alp

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 roteolysis of the proteoglycan fraction with proteinase K to significantly diminish its activity, and

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 ad antiapoptotic effect, which was lost with proteinase K treatment but not with periodate treatment.

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

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

281 Proteinase K treatment of B. burgdorferi cells decreased

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

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

284 Proteinase K treatment of intact vesicles indicates that

285 Proteinase K treatment of methanol-fixed lactobacilli el

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

287 Proteinase K treatment of the HGE agent or rP44 eliminat

288 Proteinase K treatment of the organelles shows that calp

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

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

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

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

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

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

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

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

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

298 ct nuclei and mitochondria were treated with proteinase K which traverses the pores of intact nuclei

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