ライフサイエンスコーパス: papain

1 o other related cysteine proteases (SpeB and papain).

2 ns) upon the immunization with ovalbumin and papain.

3 anonical ITAM signaling was not activated by papain.

4 t Th2 cell response to the protease-allergen papain.

5 erential proteolysis profiles of the mAbs by papain.

6 peptidic inhibitors of the cysteine protease papain.

7 and internalization of the cysteine protease papain.

8 for B cells to rapidly bind and internalize papain.

9 monstrate retrieval of the cysteine protease papain.

10 ngth Cal1 with the general cysteine protease papain.

11 inhibitors of IdeS inhibit neither SpeB nor papain.

12 but also weakly blocks the cysteine protease papain.

13 onse to immunization with the model allergen papain.

14 to prototypic proteases, namely, trypsin and papain.

15 -RAM support before and after treatment with papain.

16 iocarbazate with key active site residues in papain.

17 e result seen for the equivalent mutation in papain.

18 on using just 4 nM of the cysteine protease, papain.

19 e chia expeller by enzymatic hydrolysis with Papain.

20 r-Phe-EDANS by the proteases thermolysin and papain.

21 he S2 pocket, which is more spacious than in papain.

22 n each) but not by chymotrypsin, Pronase, or papain (0.1%, up to 2 min each).

23 Papain, a cysteine protease allergen with inherent adjuv

24 Barrier disruption by papain, a protease with structural homology to Der p 1,

25 pinna, contact sensitization, CpG, LPS, and papain all mobilized DDCs in three distinct phases: incr

26 Enzymes including papain, alpha-amylase, glucose oxidase and phytase stabi

27 f target cells with proteases (proteinase K, papain, alpha-chymotrypsin, and trypsin) abrogated entry

28 n induced by two proteases allergens HDM and papain and a classical allergen ovalbumin was evaluated

29 olled and non pH-controlled conditions using papain and a microbial-derived alternative (papain-like

30 Protease preparations from plant (papain and bromelain) and fungal (FP400 and FPII) source

31 ysed using protease preparations from plant (papain and bromelain) and fungal (FP400 and FPII) source

32 ctivities against cysteine proteases such as papain and calpain as well as the human 20S proteasome.

33 nce similarity to cysteine peptidases of the papain and calpain families.

34 ses 1, which inhibits the cysteine proteases papain and cathepsins B, K and L up to 2 times more pote

35 greater selectivity toward cathepsin L than papain and cathepsins B, K, V, and S with no activity ag

36 and disparate to the archetypical proteases papain and chymotrypsin.

37 are equally susceptible to PK and proteases papain and chymotrypsin.

38 Less effective endopin 2C inhibition of papain and elastase occurred with k(ass) association rat

39 We immunized mice in the footpad with papain and studied leukocyte recruitment and inflammator

40 work, the chia expeller was hydrolysed with Papain and the antioxidant properties of the resultant p

41 e in reducing gliadin content than the crude papain and the resultant loaves had acceptable crumb and

42 pore size of the support, and the amount of papain and time that were used for support treatment.

43 denatured RBP fractions were hydrolyzed with papain and trypsin for 3h at optimum conditions.

44 At the studied conditions, papain and trypsin were more effective in hydrolyzing Na

45 trypsin, chymotrypsin, pepsin, thermolysin, papain, and calpain.

46 ormed SDS-stable complexes with cathepsin L, papain, and elastase that are typical of serpins.

47 eases such as Pronase, proteinase K, pepsin, papain, and subtilisin.

48 A few hours after papain application, a dose-dependent reduction of EI was

49 rneum and higher cellular infiltration after papain application.

50 to cysteine proteases, such as bromelain and papain, as a model for allergens.

51 We found that papain at a range of concentrations is nearly as active

52 C) value was obtained for WP hydrolysed with papain at constant pH of 7.0 compared to the associated

53 ble type I collagen membrane were exposed to papain based gel, irradiated with laser and analyzed abo

54 t% carbamide peroxide (control); group 2, 1% papain-based whitening; group 3, 1% ficin-based whitenin

55 Overall than hydrolysates generated with papain, bromelain and FP400.

56 he range 0.8-3.2mM inhibited the activity of papain, bromelain and zingibain, iso-AA acted as an inhi

57 organic solvents, hot alkali, or proteases (papain, bromelain) diminished the adsorption rates of th

58 AA) on the activity of four plant proteases (papain, bromelain, actinidin and zingibain) and three mi

59 like cysteine proteases (clan CA, family C1) papain, bromelain, and human cathepsins L, V, K, S, F, B

60 05) by actinidin (0.8%/min) when compared to papain, bromelain, and one commercial enzyme (on average

61 different functions, including plant enzymes papain, bromelain, ficin, and mammalian lysosomal cathep

62 preparations from plant and fungal sources (papain, bromelain, FP400 and FPII) were used to hydrolys

63 d zingibain, iso-AA acted as an inhibitor of papain but as an activator of zingibain and had no signi

64 acceptors showed no cross reactivity toward papain, cathepsin B, and calpain.

65 vity with clan CA cysteine proteases such as papain, cathepsin B, and calpains.

66 Cruzain is a member of the papain/cathepsin L family of cysteine proteases, and the

67 ; and the cysteine proteases cathepsin B and papain (clan CA), and legumain (clan CD).

68 ges in near-UV CD spectra, susceptibility to papain cleavage in an adjacent CDR2 loop, and the tenden

69 or regulator released from the Fc following papain cleavage.

70 In peripheral blood lymphocytes, papain cleaved off HLA class I proteins as effectively a

71 Under conditions when papain could cut both Fab arms of non-nmAbs, only one Fa

72 plication, other eukaryotic PC synthases are papain Cys protease superfamily members but ones, unlike

73 d near that of the extensively characterized papain Cys25.

74 nduced gene silencing (VIGS), that the plant papain cysteine protease cathepsin B is required for the

75 may use a similar catalytic strategy as the papain cysteine proteases, holding its Cys184 side chain

76 Identification and analysis of Clan CA (papain) cysteine proteases in primitive protozoa and met

77 treated and control groups was quantified by papain digest and fluorescence spectrophotometry.

78 ontrol groups was quantified with the use of papain digest and fluorescence spectrophotometry.

79 on, the number of peptides identified in the Papain digest of proteins extracted with Viscozyme was a

80 and small angle x-ray scattering results of papain-digested products revealed that 1) the Fab-Fc or

81 y binds to CD105, was generated by enzymatic papain digestion and conjugated to NOTA (1,4,7-triazacyc

82 trometry-based approach, in combination with papain digestion and partial reduction, to obtain site-s

83 a combination of cation-exchange separation, papain digestion, and a panel of mass spectrometry techn

84 Papain directly activated naive T cells through protease

85 b)-tsA58/+; HRhoGFP/+) or C57BL/6 mice after papain dissociation.

86 Muller cells were isolated from papain-DNase-digested human retina.

87 family of cysteine proteinases, particularly papain (EC 3.4.22.2) itself, continue to contribute to t

88 Studies on papain (EC 3.4.22.2), the most thoroughly investigated m

89 model applications: (1) characterization of papain enzyme kinetics using rapid-mixing experiments, (

90 in invertebrates, cysteine proteases of the papain family and aspartic proteases assume the role.

91 e have now characterized five genes encoding papain family cathepsins from Toxoplasma gondii, includi

92 Falcipain-2 (FP2) is a papain family cysteine protease and important hemoglobin

93 how that CSP is proteolytically cleaved by a papain family cysteine protease of parasite origin.

94 le is a 262-amino-acid thiol protease of the papain family expressed as a combination of isoforms and

95 nhibitors of human cysteine proteases of the papain family have been made and assayed versus a number

96 Members of the papain family of cysteine cathepsins are among the prote

97 Members of the papain family of cysteine proteases (cathepsins) mediate

98 Although the papain family of cysteine proteases has been considered

99 hanism of human cathepsin K, a member of the papain family of cysteine proteases.

100 racteristically observed with members of the papain family of cysteine proteinases, help to stabilize

101 Studies on members of the papain family of cysteine proteinases, particularly papa

102 ely 130 amino acids is weakly similar to the papain family of proteases and is highly conserved from

103 Unlike other studied papain family proteases, falcipain-2 does not require it

104 e I, is a lysosomal cysteine protease of the papain family that catalyzes the sequential removal of d

105 d to cathepsin K, a cysteine protease of the papain family that is abundantly and selectively express

106 ncoding a lysosomal cysteine protease of the papain family, highly up-regulated in the developing lun

107 substrates for cysteine peptidases of the C1 papain family, important in many biological processes.

108 Cysteine proteases of the Clan CA (papain) family are the predominant protease group in pri

109 instead requires the expression of a second papain-family cathepsin protease, TgCPL.

110 udies suggest ideas for inhibitor design for papain-family cysteine proteases and strategies to progr

111 Papain, ficin and bromelain were selected out of eight f

112 ovel tooth-whitening formulations containing papain, ficin, or bromelain.

113 red in a circular permutation of the classic papain fold.

114 study intended to evaluate the effects of a papain-gel with a red-light absorbing pigment (methylene

115 Papain generated RBCF hydrolysates exhibited higher ferr

116 analysis showed that the higher activity of papain hydrolysate in most assays was related to its gre

117 for producing bioactive peptides was through papain hydrolysis and followed by 5 kDa membrane filtrat

118 water-facilitated extraction, alcalase, and papain hydrolysis, and in combination with membrane filt

119 acterized the cellular response activated by papain in basophils.

120 e challenged with house dust mite extract or papain in the absence of TSLPR have a drastic reduction

121 n of eosinophils and heightened responses to papain in the lung and increased ability to expulse the

122 virus 35S promoter)) and non-GM DNA marker (papain) in 15 min.

123 fluenza infection model in mice, and blocked papain-induced acute lung inflammation.

124 otoxin shock, and in the lung alveoli during papain-induced allergic airway inflammation.

125 tion of basophils caused a resolution of the papain-induced eosinophilia and mucus production.

126 We find that papain-induced IL-4 production requires calcium flux and

127 Interestingly, papain-induced IL-4 production was dependent on the immu

128 Papain-induced ILC2 activation and Th2 cell differentiat

129 nd the contribution of various leukocytes to papain-induced immune responses.

130 We found that during papain-induced lung inflammation, IL-9 production was la

131 eas interleukin-4 (IL-4) was dispensable for papain-induced Th2 cell differentiation, ILC2-derived IL

132 We studied how papain induces basophil migration to LNs and the contrib

133 rephthalate (PET), trehalose, and a peptide (papain inhibitor) are enhanced by 35x, 12x, and 3.5x wit

134 o displays specificity: the three identified papain inhibitors did not covalently react with UbcH7, U

135 Papain is a protease with potential use in transplantati

136 In distilled water, papain is as active in cleaving a test substrate at a te

137 This finding also holds true if papain is dissolved in Belzer-UW solution.

138 A cysteine protease, papain, is a prototypic protease allergen that can direc

139 lymerase (RdRp), the self-interaction of the papain like protease, and ORF3 interactions with the pap

140 contains a central domain homologous to the papain-like (clan CA, family C1) protease family.

141 ses: the chymotrypsin-like main protease and papain-like accessory proteases (PLpros).

142 and this part did not exhibit any effect on papain-like activities.

143 WP hydrolysed with papain-like activity under pH regulation at 7.0 displaye

144 papain and a microbial-derived alternative (papain-like activity).

145 a family of calcium-dependent proteases with papain-like activity, the calpains.

146 ribed here reveals that the protein adopts a papain-like alpha+beta fold and identifies a substrate-b

147 fungus Cryphonetria parasitica, encodes two papain-like autocatalytic leader proteases, p29 and p48,

148 Embedded in nsp1beta's papain-like autoproteinase domain, we identified a highl

149 conserved N-terminal domain and a conserved, papain-like C-terminal domain.

150 esidues, His-162 and Asp-180 of the putative papain-like catalytic triad of AtPCS1, are essential for

151 7 as a possible third member of the proposed papain-like catalytic triad.

152 s-class inhibitor with activity against both papain-like cysteine and trypsin-like serine proteinases

153 Cruzipain, the main papain-like cysteine peptidase of T. cruzi, is an import

154 howed that 4E02 targets A. thaliana vacuolar papain-like cysteine protease (PLCP) 'Responsive to Dehy

155 Two domains, X and the papain-like cysteine protease domain (PCP), of HEV ORF1

156 rotease domain, a Ca(2+)- and Zn(2+)-binding papain-like cysteine protease domain within the nonstruc

157 ooperation of a transacylating member of the papain-like cysteine protease family and an iteratively

158 phagoides pteronyssinus, that belongs to the papain-like cysteine protease family.

159 Cathepsin K, a lysosomal papain-like cysteine protease, forms collagenolytically

160 defense modulators such as terpene synthase, papain-like cysteine protease, serine carboxypeptidase,

161 o Rcr3(pim) perturbs the active site of this papain-like cysteine protease.

162 The substrate specificities of papain-like cysteine proteases (clan CA, family C1) papa

163 Papain-like cysteine proteases (PLCPs) are a large class

164 provides an increasing body of evidence for papain-like cysteine proteases (PLCPs) being central hub

165 ted effector protein Pit2 is an inhibitor of papain-like cysteine proteases (PLCPs) essential for vir

166 (GAGs) is unique for cathepsin K among human papain-like cysteine proteases and that different GAGs c

167 and relatively limited number of vertebrate papain-like cysteine proteases during blood feeding.

168 The papain-like cysteine proteases encoded by the coronaviru

169 ractionation to identify specific members of papain-like cysteine proteases involved in the N-termina

170 Cathepsins K and S are papain-like cysteine proteases with known elastolytic ac

171 ucture revealed a catalytic site typical for papain-like cysteine proteases, comprising a catalytic t

172 0, which may be significantly different from papain-like cysteine proteases.

173 The core of this structure resembles the papain-like cysteine proteases.

174 Residue Y283 is highly conserved among papain-like cysteine proteases.

175 to inhibit both chymotrypsin-like serine and papain-like cysteine proteinases.

176 is essential in blood stages and possesses a papain-like domain, prompting speculation that it functi

177 of parasitic protozoa belong to the group of papain-like enzymes known as clan CA.

178 t EPIC2B interacts with and inhibits a novel papain-like extracellular cysteine protease, termed Phyt

179 Cathepsin W is a member of the papain-like family of cysteine proteases.

180 that the Josephin domain binds Ub and has a papain-like fold that is reminiscent of that of other de

181 structure of SpvD and show that it adopts a papain-like fold with a characteristic cysteine-histidin

182 M48(USP) adopts a papain-like fold, with the active-site cysteine forming

183 frames (ORF), each encoding an autocatalytic papain-like leader protease.

184 counterparts, which, in addition to having a papain-like N-terminal catalytic domain that undergoes p

185 pressors, comprise a vertebrate subfamily of papain-like or NlpC/P60 thiol proteases that function as

186 plication depends in part on a virus-encoded papain-like protease (PL(pro)) that cleaves the viral re

187 er of the viral SARS-unique domain (SUD) and papain-like protease (PL(pro)), and, as a consequence, t

188 o 68% amino acid identity to torovirus (ToV) papain-like protease (PLP) (ToV-PLP).

189 identified as interferon (IFN) antagonists, papain-like protease (PLP) and N protein.

190 Structural studies of the papain-like protease (PLP) domains of coronaviruses (CoV

191 In this study, we focus on the SARS-CoV papain-like protease (PLP), which engages and antagonize

192 ch multifunctional domain is the coronavirus papain-like protease (PLP), which processes the viral re

193 s that are processed by two viral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpr

194 ins (nsps 1 to 16) by two viral proteases, a papain-like protease (PLpro) and a 3C-like protease (3CL

195 rs of MERS-CoV replication, we expressed the papain-like protease (PLpro) and the 3-chymotrypsin-like

196 teracting innate immunity, we identified the papain-like protease (PLpro) domain as a potent IFN anta

197 The papain-like protease (PLpro) domain from the deadly Midd

198 mmediately adjacent to the N-terminus of the papain-like protease (PLpro) domain in coronavirus polyp

199 timization of a potent inhibitor against the papain-like protease (PLpro) from the coronavirus that c

200 nhibitors with nanomolar potency against the papain-like protease (PLpro) from the SARS coronavirus (

201 cute respiratory syndrome (SARS) coronavirus papain-like protease (PLpro) is a DUB that cleaves ISG15

202 efficacy of inhibitors directed against the papain-like protease (PLpro) of severe acute respiratory

203 part of its viral genome, MERS-CoV encodes a papain-like protease (PLpro) that has been observed to a

204 ry syndrome coronavirus (MERS-CoV), encode a papain-like protease (PLpro) that possesses the ability

205 dulators encoded by the SARS-CoV genome: the papain-like protease (PLPro), nonstructural protein 1 (n

206 clude 3-chymotrypsin-like protease (3CLpro), papain-like protease (PLpro), RNA-dependent RNA polymera

207 a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro).

208 ong arteriviruses in having three N-terminal papain-like protease 1 (PLP1) domains.

209 ly linked domains of MHV nsp3, including the papain-like protease 2 (PLP2) catalytic domain, the ubiq

210 f mutations in the macrodomain (MAC) and the papain-like protease 2 (PLP2) domain of nonstructural pr

211 The coronavirus papain-like protease 2 (PLP2) domain possesses protease

212 e an ovarian tumor (OTU) domain DUB known as papain-like protease 2 (PLP2).

213 multifunctional papain-like protease, termed papain-like protease 2 (PLP2).

214 rocessing pathway independent of the encoded papain-like protease activities.

215 native processing independent of the encoded papain-like protease activities.

216 In addition to its conventional papain-like protease activity, Lpro acts as a deubiquiti

217 f ORF3 interactions with the viral helicase, papain-like protease and methylase, which suggest a regu

218 ike protease, and ORF3 interactions with the papain-like protease and putative replicase components:

219 The protein contains a papain-like protease domain (PLP2) that plays a crucial

220 Interestingly, a conserved papain-like protease domain similar to a multifunctional

221 More interestingly, we detected a conserved papain-like protease domain that commonly exists in ssRN

222 We performed bioinformatics analysis on 16 papain-like protease domains from nine different coronav

223 The SARS-CoV papain-like protease is encoded next to SUD within nonst

224 the in vivo efficacy of an inhibitor of the papain-like protease of severe acute respiratory syndrom

225 The combined results suggest that papain-like protease p48 plays an essential role in the

226 conserved domain adjacent to the coronavirus papain-like protease, altered the viral protease activit

227 Coronaviruses also possess a papain-like protease, another essential enzyme, still po

228 Coronaviruses express a multifunctional papain-like protease, termed papain-like protease 2 (PLP

229 the chimeric-virus platform to evaluate the papain-like protease/deISGylating activity of Middle Eas

230 proteins 1 to 3 are processed by one or two papain-like proteases (PLP1 and PLP2) at specific cleava

231 polyprotein 1a is predicted to encode three papain-like proteases (PLP1alpha, PLP1beta, and PLP1gamm

232 locking the secrets of how coronavirus (CoV) papain-like proteases (PLpros) perform their multifuncti

233 s multiple structural domains, including two papain-like proteases (PLPs) and a highly conserved ADP-

234 oronavirus (MERS-CoV) encode multifunctional papain-like proteases (PLPs) that have the ability to pr

235 ase gene products and characterize two viral papain-like proteases (PLPs), PLP1 and PLP2, which proce

236 roteases via its carboxy-extended domain and papain-like proteases by its amino-terminal domain.

237 scribe a novel tool for studying the role of papain-like proteases in diverse biologic phenomena and

238 Rcr3 and Pip1 are paralogous secreted papain-like proteases of tomato.

239 e position of the canonical catalytic Cys of papain-like proteases, and the function of SERA5 or whet

240 ation of proteins, and viral multifunctional papain-like proteases, enzymes that cleave polyproteins

241 fungus Cryphonectria parasitica, encodes two papain-like proteases, p29 and p48.

242 d on analogy with inhibitor complexes of the papain-like proteases, we propose a model for the substr

243 (MHV), nsps 1, 2, and 3 are processed by two papain-like proteinase activities within nsp3 (PLP1 and

244 domain located immediately downstream of the papain-like proteinase domain.

245 ensively processed by three proteinases, two papain-like proteinases (PLPs), termed PLP1 and PLP2, an

246 to proteolytically modify the SERA family of papain-like proteins.

247 ole OcXII gene presented higher legumain and papain-like proteolytic activities, resulting in a faste

248 in Z, which are both cysteine proteases of a papain-like structure.

249 s from other sources have the hallmarks of a papain-like, Clan CA Cys protease.

250 After exposure to the natural allergen papain, mice selectively lacking the miR-17 approximatel

251 Peanut kernels were treated by Alcalase, papain, Neutrase and bromelain, respectively.

252 immunization with ovalbumin (OVA) along with papain or alum.

253 EKTI did not inhibit the cysteine proteinase papain or cathepsin K, L, or S.

254 ective inhibition of cathepsin L compared to papain or elastase.

255 ce interleukin 13 (IL-13) when stimulated by papain or house dust mite extract (HDM) and induce eosin

256 eras were treated with the protease allergen papain or the cytokines IL-25 and IL-33 or infected with

257 rface of the support then being treated with papain (or a related agent) to release and remove their

258 sted with proteases such as trypsin, pepsin, papain, or endopeptidase Gly-C.

259 Tooth bleaching gels containing bromelain, papain, or ficin have substantial clinical potential to

260 Sensitization to protease allergens, such as papain, or helminth infection is associated with basophi

261 eg cells, thereby suppressing development of papain- or IL-33-induced airway eosinophilia.

262 Sodium caseinate (NaCas) was hydrolyzed by papain, pancreatin and trypsin from 10 min to 24h, and t

263 Subcutaneous immunization with papain plus antigen induced reactive oxygen species (ROS

264 ase (CpL-PME; EC 3.1.1.11) from a commercial papain preparation.

265 nd then hydrolyzed with proteases (Alcalase, Papain, Protamex, Flavourzyme).

266 ubiquitin recognition and a variation on the papain protease catalytic site configuration that appear

267 Although a member of the papain protease superfamily, Gly m Bd 30 K has a glycine

268 ven within these families of proteins (e.g., papain-related Cys-dependent hydrolases and rhodanese/Cd

269 -Lys-Thr-Phe-Cys]-OH (11), starting with the papain-resolved Fmoc-DAgl(Boc).

270 We test papain's HLA class I removing activity under recognized

271 The mechanism of papain's immunogenic activity remains unknown.

272 The activity of papain's substrate selectivity was tested using both a t

273 These findings suggest that papain's targeted enzymatic cleavage of donor HLA class

274 olysates, Viscozyme-proteins hydrolyzed with Papain showed the highest ability to quench ABTS(+) radi

275 ion, the effects of mutations in 23 genes on papain-specific IgE or IgG1 were verified.

276 Intranasal administration of papain stimulated ILC2s and Th2 cells, causing allergic

277 btilisin subfamilies of serine proteases and papain subfamily of cysteine proteases.

278 Finally, studies with the cysteine protease, papain, suggest that the reduction of sulfinamide to the

279 Cysteine proteases of the papain superfamily are implicated in a number of cellula

280 psin S, a lysosomal cysteine protease of the papain superfamily, has been implicated in the preparati

281 psin K, a lysosomal cysteine protease of the papain superfamily, is abundantly and selectively expres

282 t induce T helper type 1 (Th1) responses, or papain that induces T helper type 2 (Th2) responses.

283 xpanded in response to the protease allergen papain, they produced ILC3 but not ILC2 cytokines and ca

284 , and the captured material was treated with papain to generate Fab and Fc for LC/MS analysis.

285 se ADCs involve cleavage with cathepsin B or papain to release and measure the antibody-conjugated dr

286 lease the MNPs, however addition of 20 nM of papain to the urine samples resulted in a time-dependent

287 rotocols for cryopreservation of ejaculated, papain-treated alpaca spermatozoa.

288 hembras were inseminated with either fresh, papain-treated or frozen-thawed spermatozoa.

289 Pregnancy can be achieved after AI with papain-treated spermatozoa.

290 (n = 26) were not different (1/5 fresh, 1/4 papain-treated, 0/17 frozen-thawed; P = 0.10).

291 Papain treatment of the chia seed expeller demonstrated

292 Papain-triggered innate immune responses were dependent

293 lter cell surface charge, including trypsin, papain, tunicamycin, neuraminidase, and polybrene, allow

294 The activity of papain was also tested at 4 degrees C, the temperature o

295 ctivated receptor (PAR)-2; TSLP induction by papain was partially dependent on PAR-2.

296 Papain was the enzyme of choice, based on in silico anal

297 water fish (Cirrhinus mrigala) muscle, using papain, were investigated.

298 f IdeS are even more potent as inhibitors of papain, whereas smaller analogues that are active inhibi

299 of dionain-1 was largely similar to that of papain with a preference for hydrophobic and aliphatic r

300 erlase (WPH-Ever; zeta-potential, -39mV) and papain (WPH-Pap; zeta-potential, -7mV), during simulated