ライフサイエンスコーパス: degreesC

1 rface temperature has increased by about 1.0 degreesC over the past five centuries.

2 structure by 0.4 to 0.75 kcal/mol (pH 7.4, 0 degreesC, 0.35 M ionic strength) and often produces cros

3 y 1.39 kcal/mol for DeltaG degrees37 and 7.0 degreesC for the TM.

4 except Gsalpha-E259V bind to beta gamma at 0 degreesC and were stable at higher temperatures.

5 Incubation at 0 degreesC or in the presence of 2 mM KCN abolished high-a

6 ion revealed enhanced complex formation at 0 degreesC when the DNA is missing nucleosides in two broa

7 has a much longer dissociation lifetime at 0 degreesC.Based on footprinting, kinetic and thermodynami

8 temperature downshift from 37 degreesC to 0 degreesC.

9 esC and (transiently) after a downshift to 0 degreesC; (ii) does opening of the start site region in

10 biphasic process (k = 0.1 and 0.01 s-1 at 10 degreesC) in the absence of these molecules.

11 of 1.25 x 10(-)3 mM-1 s-1 and 128 s-1 at 10 degreesC, respectively) that was stable in the presence

12 e-chains in the temperature range from 5-100 degreesC.

13 ophilic archaeon that grows optimally at 100 degreesC by the fermentation of peptides and carbohydrat

14 At 100 degreesC, the growth temperatures of the hyperthermophil

15 in the probe of an NMR spectrometer at -100 degreesC.

16 ilic archaeon which grows optimally near 100 degreesC by fermenting peptides and sugars to produce or

17 se, which is a strong glass former (Tg = 115 degreesC), elevates the onset of the lipid headgroup rot

18 ype level) at 45 degreesC to nearly 25 at 13 degreesC.

19 rmal melting temperature for P41 which is 13 degreesC lower than that for P46 and the unfolding of P4

20 e warm (mean annual temperature exceeding 14 degreesC) rather than near freezing.

21 l structures containing ERGIC-53 during a 15 degreesC treatment, suggesting that it is a cycling prot

22 inetic parameters have been determined at 15 degreesC and pH 7.2 in a stopped-flow spectrophotometer;

23 Cells stained at 15 degreesC for both FM4-64 and carboxydichlorofluorescein

24 ot actively take up nitrate or nitrite at 15 degreesC, although nitrate reductase and nitrite reducta

25 ensity (250 microE m-2 s-1) for growth at 15 degreesC.

26 f the activity at 38 degreesC remained at 15 degreesC.

27 at high light intensity (3 mE m-2 s-1) at 15 degreesC.

28 reasing temperature, and growth ceased at 15 degreesC.

29 ddition, we find that at low temperature (15 degreesC), cells contain a pool of nontranslating riboso

30 We show that incubation at 16 degreesC blocks passage of endocytosed transferrin into

31 it recycling of molecules interiorized at 16 degreesC is consistent with their recycling taking place

32 ng of molecules that were interiorized at 16 degreesC.

33 with transferrin at either 37 degreesC or 16 degreesC.

34 tertiary structure with a Tm of 76.0 +/- 0.2 degreesC and no appreciable loss of the secondary struct

35 DE predominantly are in the wobble form at 2 degreesC.

36 o the more global effect of cooling RCs to 2 degreesC in the absence of Zn(II).

37 e temperature oscillations of 1 degrees to 2 degreesC increase in size to approximately 4 degrees to

38 concentrations at two temperatures (6 and 20 degreesC) demonstrated that the population formed during

39 -243, and -227 mV (+/-5 mV) at pH 7.0 and 20 degreesC, respectively.

40 at trpt was estimated to be near zero at 20 degreesC and at about 45% at 37 degreesC.

41 e other double mutants after treatment at 20 degreesC in a pattern generally supporting that indicate

42 onitor assay for 180 days when stored at -20 degreesC or for 60 days at 4 degreesC.

43 e average alpha-helical content of CaM at 20 degreesC.

44 ect of missing nucleosides was evident at 20 degreesC.

45 ate was too fast to measure accurately at 20 degreesC; the second intermediate formed with a rate con

46 is 80% alpha-helical and stably folded at 20 degreesC; thermal denaturation is first detected at 70 d

47 s sp. PCC 6301 grew exponentially between 20 degreesC and 38 degreesC, the growth rate decreased with

48 ly of the G4 capsid at temperatures above 21 degreesC.

49 aCl2 at ionic strength 0.15 M, pH 7.0 and 21 degreesC.

50 ng nucleotide of 26, 49, and 24 microM at 21 degreesC, respectively, for the wild type and its active

51 r maintaining elevated body temperatures (21 degreesC above ambient) and attaining large size (up to

52 amperometric events was much lower at 21-22 degreesC than at 32-35 degreesC.

53 nd temperature control groups in cages at 22 degreesC and 28 degreesC.

54 an the range from 2.75 to -25.1 mL/mol at 22 degreesC and pH* 7.5.

55 sition were similar (kapp = 0.04 min-1 at 22 degreesC for both), the kapp for corresponding vesicles

56 e was 20-fold less (kapp = 0.002 min-1 at 22 degreesC).

57 id binding protein (I-FABP) at pH 5.5 and 23 degreesC, and, for comparison, on PA incorporated into 1

58 lalanine, 120 microM DMPH4 and pH 7.4 and 23 degreesC.

59 as shown that Arg-DHFRts is long-lived at 23 degreesC but short-lived at 37 degreesC in the yeast Sac

60 the metabolic stability of Arg-DHFRts at 23 degreesC results, at least in part, from steric inaccess

61 12 micromol of TXA2/min/mg of protein at 23 degreesC.

62 nd has a half-life in air of about 1 h at 23 degreesC.

63 eltaK-DHFRts was rapidly degraded at both 23 degreesC and 37 degreesC.

64 recPOR-delta (-403 +/- 8 mV at pH 8.0 and 24 degreesC) decreased linearly with temperature (-1.55 mV/

65 icate that the framework is stable up to 240 degreesC.

66 tic studies at pH 7.49 (Hepes, 20 mM) and 25 degreesC showed that the most active antibody, MATT.F-1,

67 10(6) M-1 min-1 at pH 7.4, mu = 0.1 M and 25 degreesC.

68 stant of less than 1 microM at pH 7.0 and 25 degreesC.

69 were normally maintained at approximately 25 degreesC.

70 s found to be approximately 0.0002 s-1 at 25 degreesC by SPR.

71 been conducted in pH 7.4 Hepes buffer at 25 degreesC on the removal of Fe(III) and Al(III) from the

72 At 25 degreesC, the H2O2-supported reaction had a specific act

73 At 25 degreesC, the stability estimate obtained by extrapolati

74 s grown on a fermentable carbon source at 25 degreesC, while dihydrosphingosine-1-phosphate (DHS-1-P)

75 IMP causes only a slight inhibition at 25 degreesC.

76 n the absence of denaturant of 0.8 s-1 at 25 degreesC.

77 -6 min-1 for AChE and 2 min-1 for BChE at 25 degreesC.

78 ilities but similar CO2 permeabilities at 25 degreesC.

79 ng, Delta GH-2O/D-N, of 3.1 kcal mol-1 at 25 degreesC.

80 +/-0.5) x 10(8) M-1 (pH 7.0, 0.20 M NaCl, 25 degreesC).

81 cubated at 90 degreesC and then cooled to 25 degreesC were capable of rebinding to, and of reactivati

82 3-week-old postnatal rats recorded at 24-26 degreesC.

83 reasingly uncoupled from H+ pumping above 28 degreesC.

84 ontrol groups in cages at 22 degreesC and 28 degreesC.

85 f folding in water, kfH2O, is 0.23 s-1 at 28 degreesC and, at urea concentrations above 1 M, the fold

86 enance of these transfected cell lines at 28 degreesC resulted in localization of the H1069Q protein

87 ering of induction temperature from 37 to 28 degreesC (in the case of T265R-alpha), however, resulted

88 ees, and TM within 3.2%, 6.0%, 6.8%, and 1.3 degreesC, respectively.

89 frequent complications were temperature>38.3 degreesC (54%), followed by anemia treated with transfus

90 nterconversion over a temperature range of 3 degreesC to 49 degreesC, allowing characterization of th

91 procollagen lacking the D1 period unfolded 3 degreesC lower than a full-length molecule.

92 terminal D0.4 period, the protein unfolded 3 degreesC lower than the full-length molecule and a small

93 However, at 30 degreesC in vitro, both Delta1-10 and Delta1-11 showed c

94 ng protein of Saccharomyces cerevisiae at 30 degreesC, in buffers ranging in salt concentration from

95 ible inactivation of the alpha subunit at 30 degreesC.

96 However, at temperatures below 30 degreesC or when refolding begins from an equilibrium in

97 ing free energy that is unfavorable below 30 degreesC.

98 and depresses the melting temperature by 30 degreesC, presumably by binding to the unfolded form of

99 However, following hypothermic (30 degreesC) reperfusion, both respiration rates and all en

100 binding is transient at low temperature (<30 degreesC) and stable at high temperature (>35 degreesC).

101 elded new mesophiles (optimal growth near 30 degreesC) that produce heparin-like exopolysaccharides o

102 At 1 mM Mg2+, a DeltaTm of 30 degreesC was observed for pdU- versus T-containing 15-me

103 and 2 h of reperfusion at 37 degreesC or 30 degreesC.

104 from 10 degrees C (Kd = 618 +/- 34 nM) to 30 degreesC (Kd = 334 +/- 15 nM), and again from 30 to 50 d

105 ies (at pH over 1.3 and temperature under 30 degreesC) but not in important subsurface acid-forming e

106 s pH 7.5, and the temperature optimum was 30 degreesC.

107 When slices were incubated at 31 degreesC (hypothermia) during OGD/reoxygenation, neurona

108 at fusion of inclusions does not occur at 32 degreesC in multiple mammalian cell lines and with three

109 y was produced in host cells incubated at 32 degreesC, and the unfused inclusions remained competent

110 ndosomes were unaffected by incubation at 32 degreesC.

111 on is Ino2p-dependent in NMT1 cells at 24-33 degreesC.

112 returned to the permissive temperature of 33 degreesC, these same cells make a significant amount of

113 at room temperature and those recorded at 34 degreesC, and strontium could be substituted for calcium

114 s much lower at 21-22 degreesC than at 32-35 degreesC.

115 l conditions for activity were pH 7.8 and 35 degreesC.

116 ual temperature-sensitive conformation at 35 degreesC that allowed cleavage at an otherwise resistant

117 was unable to grow photosynthetically at 35 degreesC, but it expressed a substantial level of Rubisc

118 opy of nmt487D will not support growth at 35 degreesC, survival of HMC1 depends upon its human Nmt.

119 Mild hypothermia (33 degrees-35 degreesC) can ameliorate brain edema after traumatic bra

120 egreesC) and stable at high temperature (>35 degreesC).

121 ozen-thawed brain tissue sections at 0 or 35 degreesC.

122 ide (HOOH) in phosphate buffer at pH 7.0, 37 degreesC.

123 he bases as a function of temperature (20-37 degreesC).

124 iological ionic strength buffers (pH 7.5, 37 degreesC) WT Hsp104 exhibits Michaelis-Menten kinetics b

125 bation at physiological conditions (pH 7, 37 degreesC) presented a linear increase in chemiluminescen

126 um acetate at 33 degrees, 35 degrees, and 37 degreesC or vehicle at 37 degreesC.

127 slowly than the wild type at both 18 and 37 degreesC.

128 nced the uptake of 125I-LDL at both 4 and 37 degreesC.

129 greesC at the same rate as between 25 and 37 degreesC.

130 mp technique at both room temperature and 37 degreesC.

131 rapidly degraded at both 23 degreesC and 37 degreesC.

132 he transcription start site (RPo) both at 37 degreesC and (transiently) after a downshift to 0 degree

133 = -0.7) was identical to that for abg at 37 degreesC and implies that these enzymes utilize nearly i

134 lexes populated at binding equilibrium at 37 degreesC and transiently populated at a fixed time after

135 ls and then followed their trafficking at 37 degreesC by indirect immunofluorescence.

136 tes irreversible inactivation of alpha at 37 degreesC despite the presence of beta gamma.

137 S. cerevisiae, Arg-DHFRts is degraded at 37 degreesC exclusively by the N-end rule pathway, whereas

138 is 15-fold higher at 75 degreesC than at 37 degreesC in keeping with the thermophilicity of the orga

139 This kinetic trap is avoidable at 37 degreesC in the circularly permuted RNA.

140 g-lived at 23 degreesC but short-lived at 37 degreesC in the yeast Saccharomyces cerevisiae.

141 by SNG following incubation for 30 min at 37 degreesC is 200-400 microM.

142 now compared the effects on recycling at 37 degreesC of overexpression of wild-type rab11 and variou

143 dney (NRK) epithelial cells maintained at 37 degreesC on the microscope stage resulted in a very rapi

144 rotid occlusion and 2 h of reperfusion at 37 degreesC or 30 degreesC.

145 BFTE cells were pretreated for 60 min at 37 degreesC prior to inoculation.

146 Cell-free transcription/translation at 37 degreesC showed mutants deleted through residue 9 were e

147 um in the presence or absence of cells at 37 degreesC showed that the recombinant proteins were as st

148 of *NO-sGC in the presence of 1 mM GSH at 37 degreesC was 6.3 min.

149 ce of ATPgammaS (kcat = 1 x 10(-4) s-1 at 37 degreesC), demonstrate that upon interaction with ATP th

150 ctors of -35.1+/-1.3 and -5.4+/-0.4 mV at 37 degreesC, and -37.6+/-1.8 and -5.8+/-0.6 mV at room temp

151 ells is rapidly degraded, particularly at 37 degreesC, but can be protected from degradation by prior

152 ] are temperature sensitive for growth at 37 degreesC, demonstrating a requirement for this domain fo

153 F1.GTP first primes the Golgi membrane at 37 degreesC, followed by AP-1 binding on ice, we find that

154 ctivation with a half-life of 9.3 days at 37 degreesC, suggesting that the mutant is still capable of

155 reasing concentrations of Triton X-100 at 37 degreesC, the electron transfer activity decreases, wher

156 y reported to be essential for binding at 37 degreesC, were found not to be critical for binding at 4

157 M Tris-HCl (pH 7) or upon reincubation at 37 degreesC, whereas AP-1 recruited with GTPgammaS or by a

158 e seconds) than the wild-type ribozyme at 37 degreesC.

159 t (6-40 ps) motions and slower motions at 37 degreesC.

160 less rapidly inactivated by incubation at 37 degreesC.

161 r zero at 20 degreesC and at about 45% at 37 degreesC.

162 HCl buffer at neutral pH (6.5-8.5) and at 37 degreesC.

163 time constants of approximately 100 ms at 37 degreesC.

164 slocation and transcriptional function at 37 degreesC.

165 ured than those with A.T/T.A neighbors at 37 degreesC.

166 the chaperonin as the folded conformer at 37 degreesC.

167 e nucleolus, but conferred slow growth at 37 degreesC.

168 ad a half-life of approximately 90 min at 37 degreesC.

169 35 degrees, and 37 degreesC or vehicle at 37 degreesC.

170 dominantly in an unfolded conformation at 37 degreesC.

171 ith none occurring in strains cultured at 37 degreesC.

172 g the whole-cell patch-clamp technique at 37 degreesC.

173 ivation abilities by both p73 isoforms at 37 degreesC.

174 ad been loaded with transferrin at either 37 degreesC or 16 degreesC.

175 d time after a temperature downshift from 37 degreesC to 0 degreesC.

176 was 0.033 +/- 0.005 cm/s (SE, n = 6 mice, 37 degreesC), much lower than that of 0.15 +/- 0.03 cm/s (n

177 After normothermic (37 degreesC) ischaemia/reperfusion, significant decreases i

178 owth at the non-permissive temperature of 37 degreesC.

179 ccur in parental CHO cells at either 0 or 37 degreesC and was inhibited by addition of 0.25 M sucrose

180 tated by higher pH (7.0) and temperature (37 degreesC) and by the presence of L-subunit and is comple

181 - phenotype only at elevated temperature (37 degreesC).

182 by shifting the infected cells from 32 to 37 degreesC allowed the measurement of the rate and the tim

183 mined after temperature shifts from 28 to 37 degreesC and from 37 to 40 degreesC.

184 Shifting cells to 37 degreesC causes transient eight- and fivefold increases

185 perature identically to growth rate up to 37 degreesC.

186 hereas the reverse was true after a 28-to-37 degreesC temperature shift.

187 rew exponentially between 20 degreesC and 38 degreesC, the growth rate decreased with decreasing temp

188 ate, and more than 20% of the activity at 38 degreesC remained at 15 degreesC.

189 cence from cells stained at 30 degrees or 38 degreesC.

190 At 39 degreesC, the E1B 55-kDa mutant viruses produced wild-ty

191 At the nonpermissive temperature of 39 degreesC, scid pre-B cell lines fail to form coding join

192 ry structures with Tm values of 74.8 +/- 0.4 degreesC and 74.3 +/- 0.7 degreesC, respectively, under

193 st complementary RNA showed increases of 3-4 degreesC per modification for single substitutions and s

194 t of (8.5 +/- 4.4) x 10(6) M-1 (pH 7.0 and 4 degreesC).

195 At 4 degreesC and pH 7.5, stability was found to be strongly

196 In contrast, storage of platelets at 4 degreesC caused a significant reduction in their life sp

197 Inasmuch as the overall turnover number at 4 degreesC is 62 s-1, the covalent intermediate is kinetic

198 sumption measurements, varies from 22.5 at 4 degreesC to 13 at 45 degreesC, consistent with tunneling

199 ally and with high affinity (Kd = 6 nM) at 4 degreesC to bovine aortic endothelial cells, increasing

200 ted proteolytic cleavage during storage at 4 degreesC to generate two fragments of 28 and 8 kDa.

201 rst ATP turnover (kcat = 4 x 10(-3) s-1 at 4 degreesC), or in the presence of ATPgammaS (kcat = 1 x 1

202 The enzyme is routinely stored at 4 degreesC, in 0.05 m Tris/HCl buffer containing 25% glyce

203 ognition helix (alphaA) is well-defined at 4 degreesC, whereas the other (alphaB) is disordered but i

204 A heme oxygenase in their ferric states at 4 degreesC.

205 recombinant polypeptide during storage at 4 degreesC.

206 se upon cleavage of N-terminal residues at 4 degreesC.

207 re found not to be critical for binding at 4 degreesC.

208 n stored at -20 degreesC or for 60 days at 4 degreesC.

209 after storage for approximately 5 days at 4 degreesC.

210 50 to 400 microM and at temperatures from 4 degreesC to 40 degreesC.

211 e linear template at pH 7.5, 200 mM MgCl2, 4 degreesC.

212 At 37 but not 4 degreesC, the cells also hydroxylated the label to 5, 20

213 e when placed at an ambient temperature of 4 degreesC, suggesting that different thresholds exist for

214 lly after reducing it to 5-[3H]HETE (37 or 4 degreesC).

215 e varying metabolic reactions, PMNs (37 or 4 degreesC; +/- triacsin C) could not be shown to receptor

216 monodansylcadaverine, and low temperature (4 degreesC) inhibited the internalization of P. intermedia

217 ersistence length for the low temperature (4 degreesC), stacked form is 78 (+/-8) A for a helix rise

218 o proceeds rapidly and quantitatively at -40 degreesC.

219 2-chlorophenyl) phosphorochloridate 5 at -40 degreesC; it is followed by in situ treatment with 2-(4-

220 nism of acute-phase protein regulation at 40 degreesC.

221 mol/dm3sodium acetate buffer (pH 4.0) at 40 degreesC.

222 ermined by NMR was approximately 2 s-1 at 40 degreesC.

223 populated, reaching approximately 40% at 40 degreesC.

224 oM and at temperatures from 4 degreesC to 40 degreesC.

225 fts from 28 to 37 degreesC and from 37 to 40 degreesC.

226 er than those of HSP60 mRNA after a 37-to-40 degreesC temperature shift, whereas the reverse was true

227 t emerged for temperatures between 20 and 41 degreesC at similar surface pressures 6-8 mN/m higher th

228 a helix-to-coil transition between 25 and 42 degreesC as assayed by circular dichroism.

229 omosomal topA mutation in E. coli AS17 at 42 degreesC, possibly accounting for the conservation of th

230 rongly induced by incubating parasites at 42 degreesC.

231 hed at a pH of 6.25, and a temperature of 42 degreesC.

232 In contrast, in htrB mutants shifted to 42 degreesC for 3 h, tetra-acylated lipid A species and gly

233 mperature is increased from 8 degreesC to 42 degreesC, at which temperature either protein is complet

234 er the temperature range of 8 degreesC to 42 degreesC, GroEL binds MuDHFR more tightly than EcDHFR, d

235 several pretreatments: (1) hyperthermia (43 degreesC), (2) 60-Hz, 8- microT EM fields, or (3) 60-Hz,

236 HS-1-P levels, grow slowly, and survive a 44 degreesC heat stress 10-fold better than parental cells.

237 strain (designated TG1/pTAG1) is grown at 44 degreesC, the plasmid bearing the lpxK+ is lost, and the

238 ) accumulated in TG1/pTAG1 cells grown at 44 degreesC.

239 ongation rate continues to increase up to 44 degreesC at the same rate as between 25 and 37 degreesC.

240 rmed by enzyme reactions performed over 0-45 degreesC.

241 C) at temperatures between 30 degrees and 45 degreesC that span the main phase transition of DPPC.

242 ation, differential growth at 37, 42, and 45 degreesC, identification by API 20C, fluorescence, chlam

243 optimum enzymatic activity at pH 10.0 and 45 degreesC.

244 rate, from ca. 5 (the wild-type level) at 45 degreesC to nearly 25 at 13 degreesC.

245 , varies from 22.5 at 4 degreesC to 13 at 45 degreesC, consistent with tunneling being involved in th

246 pH of 7 to 7.5, an optimum temperature of 45 degreesC, and an optimal divalent-cation concentration o

247 over a temperature range of 3 degreesC to 49 degreesC, allowing characterization of the thermodynamic

248 ild-type Arabidopsis was increased from -5.5 degreesC to -12.6 degreesC by cold acclimation whereas t

249 s, animals treated with methamphetamine at 5 degreesC showed DA release identical to that of animals

250 more stable than the unmodified hairpin by 5 degreesC, and this corresponds with increased base stack

251 administered at an ambient temperature of 5 degreesC, no increase in dopamine oxidation products was

252 thermal denaturation at approximately 45-50 degreesC, as shown by the appearance of amide I bands at

253 ile, (ii) concentrated aqueous ammonia at 50 degreesC and (iii) 0.5 mol/dm3sodium acetate buffer (pH

254 from SfiI reactions on supercoiled DNA at 50 degreesC yielded a helical repeat of about 11.5 base-pai

255 lysozyme or bovine insulin) at 23, 37, or 50 degreesC, leading to covalent incorporation of the ligan

256 (pH 0.3 to 0.7, temperature 30 degrees to 50 degreesC).

257 f the mutant enzyme was linear from 20 to 50 degreesC.

258 ene cation exchange column at pH 5.27 and 55 degreesC.

259 volatilized by treatment with 2 M NaOH at 55 degreesC for up to 48 h, suggesting that they were not m

260 hasic melting, with transitions at 28 and 56 degreesC.

261 calcination of the organic component at 575 degreesC.

262 ant lines ranged from -6.8 degreesC to -10.6 degreesC in the absence of acclimation.

263 is was increased from -5.5 degreesC to -12.6 degreesC by cold acclimation whereas the freezing tolera

264 modified and unmodified RNA hairpins by 5-6 degreesC, and decreases the DeltaG degrees for hairpin f

265 ease in size to approximately 4 degrees to 6 degreesC, and catastrophic iceberg discharges begin alte

266 rsible thermal unfolding at approximately 60 degreesC.

267 secondary structure is retained, even at 60 degreesC, consistent with a partially unfolded "molten g

268 a direct methanol fuel cell operating at 60 degreesC, even though the latter catalyst had about twic

269 The tm for the wild-type RNA is 60 degreesC; for the double-deletion mutant U2653Delta/C266

270 n inhibitor at more extreme conditions of 60 degreesC and pH* 8 where major unfolding events or struc

271 letion mutant U2653Delta/C2667Delta it is 65 degreesC; and for the U2653G transversion it is 69 degre

272 sC; and for the U2653G transversion it is 69 degreesC.

273 es of 74.8 +/- 0.4 degreesC and 74.3 +/- 0.7 degreesC, respectively, under analogous conditions in wa

274 toplasts frozen over the range of -4.5 to -7 degreesC.

275 thermal denaturation is first detected at 70 degreesC.

276 from mesophiles, with maximum activity at 70 degreesC.

277 ly low propylene concentrations at 50 and 75 degreesC, where stereoerrors attributable to chain epime

278 SC, RN, and H30A were very stable at 75 degreesC (pH 8.0), with half-lives of 4.7, 2.8, and 2.7

279 e rate of hydrolysis is 15-fold higher at 75 degreesC than at 37 degreesC in keeping with the thermop

280 lar, SC is more stable to inactivation at 75 degreesC, and less susceptible to inactivation by phenyl

281 olerance of 26 mutant lines ranged from -6.8 degreesC to -10.6 degreesC in the absence of acclimation

282 eases as the temperature is increased from 8 degreesC to 42 degreesC, at which temperature either pro

283 Over the temperature range of 8 degreesC to 42 degreesC, GroEL binds MuDHFR more tightly

284 at 80 degreesC), and the apparent Kms (at 80 degreesC) for ethanol, acetaldehyde, NADP, and NAD were

285 own subunit (apparent Km = 1.0 microM at 80 degreesC) than for Fd (apparent Km = 4.4 microM).

286 ol oxidation was between 9.4 and 10.2 (at 80 degreesC), and the apparent Kms (at 80 degreesC) for eth

287 st activity over 4-5 days when stored at -80 degreesC in the presence of CL, but reached a level of a

288 d enzymes stored in the absence of CL at -80 degreesC were much less active, the enzymes retained thi

289 cardiolipin after 8-9 days of storage at -80 degreesC without cardiolipin.

290 pHAS and seHAS were stored without CL at -80 degreesC, even after 2 months, they could be stimulated

291 zyme retains full activity when heated to 80 degreesC, and the rate of hydrolysis is 15-fold higher a

292 th temperature (-1.55 mV/ degreesC) up to 82 degreesC.

293 ble loss of the secondary structure up to 85 degreesC.

294 A57 and DrrA have apparent Tm's of 75 and 90 degreesC, respectively.

295 plexes thermally denatured between 70 and 90 degreesC.

296 ines to olefins at temperatures as low as 90 degreesC.

297 anganese stabilizing protein incubated at 90 degreesC and then cooled to 25 degreesC were capable of

298 gh temperature, with half-lives at 85 and 95 degreesC of 160 and 7 h, respectively.

299 The Bronsted coefficient for bgl at 95 degreesC (beta1g = -0.7) was identical to that for abg a

300 creased linearly with temperature (-1.55 mV/ degreesC) up to 82 degreesC.