ライフサイエンスコーパス: Bmax

1 Bmax was also inversely related to harsh parenting; boys

2 Bmax was not related to boys' disruptive behavior.

3 Bmax was significantly lower in boys whose parents had h

4 Bmax/Kd (ratio of the distribution volumes in striatum t

5 cantly lower D2 receptor levels (mean = 2.72 Bmax/Kd, SD = 0.3) than subjects who disliked its effect

6 ly transfected with hCTR2 (125I-hCAL = 24.8% Bmax, 125I-rAmylin = 8% Bmax).

7 2 (125I-hCAL = 24.8% Bmax, 125I-rAmylin = 8% Bmax).

8 GR binding sites having a Kd of 290 nM and a Bmax of 1.3 pmole/mg protein.

9 ng isotherm with a Kd of 140 +/- 60 nM and a Bmax of 118 fmol per 10(5) cells.

10 cells with a Kd of 0.064 +/- 0.006 nM and a Bmax of 244 +/- 12 fmol/mg protein.

11 10-lysylbradykinin with a Kd of 0.3 nM and a Bmax of 38 fmol/mg protein ( approximately 40,000 recept

12 es, with an affinity of 2.7 +/- 0.9 nM and a Bmax of 4.8 x 10(4) binding sites per cell.

13 studies indicated a Kd of 99 +/- 6 pM and a Bmax of 45 +/- 4 fmol/mg membrane protein.

14 platelet membranes with a Kd of 15 nM and a Bmax of 5.2 pmol/mg of protein.

15 und with an affinity (Kd) of 24 microM and a Bmax of 53 x 106 binding sites/cell at 37 degrees C.

16 red with an affinity (Kd) of 37 microM and a Bmax of 65 x 106 binding sites/cell at 37 degrees C.

17 indicated a Kd of approximately 0.8 nM and a Bmax of approximately 32 fmol/mg protein.

18 muscle with a Kd value of 37 +/- 3 nM and a Bmax value of 280 +/- 14 fmol/mg of protein.

19 atidine with a Kd value of 304+/-16 pM and a Bmax value of 8942 +/- 115 fmol/mg protein.

20 This population has a Bmax of 18 +/- 7 microg/mg and a Kd of 25 +/- 9 nM.

21 al beta2-AR (4230 receptors per cell) with a Bmax at 129.3 and a KD of 3.19 nM but lack beta1-AR expr

22 specific [3H]bradykinin-binding sites with a Bmax of 271 fmol/mg protein and a Kd of 0.83 nmol/l.

23 affinity, exhibiting a Kd of 34.3 nM with a Bmax of 441 fmol/mg protein.

24 xhibiting a Kd of approximately 32 nM with a Bmax of 550 fmol/mg protein in both animals.

25 IDC, PPH, and NF right ventricles (RV), ACE Bmax was 737+/-78, 638+/-137, and 422+/-49 fmol/mg, resp

26 KD) and maximum binding capacity of analyte (Bmax) values for the interaction of complementary DNA ta

27 KD) and maximum binding capacity of analyte (Bmax) values for the interaction of MoabPf or PoabPf wit

28 002; E2: -20.7%+/-11.7%, P < or = 0.007) and Bmax/Kd (E1: -18.4%+/-8.7%, P < or = 0.002; E2: -13.4%+/

29 of [(3)H]U69,593 to KOR showed that K(d) and Bmax values were not significantly affected by prior in

30 The Kd and Bmax of TR2-11-f homodimer binding to this direct repeat

31 y (Kd, 3 x 10(-7) M versus 5 x 10(-8) M) and Bmax (1.9 x 10(5) versus 7.9 x 10(5)) compared with BAD1

32 InsP3 binding experiments (KD = 23.6 nM and Bmax = 0.46 pmol/mg) suggest the myocytes contain the hi

33 sites for EGF with Kd = 1.78 +/- 0.26 nM and Bmax = 216.8 +/- 19.6 fmol/mg membrane protein were also

34 high affinity site (Kd = 2.3 +/- 0.9 nM and Bmax = 55.5 +/- 8.1 pmol/g tissue) with a pharmacologica

35 inding sites, exhibiting a Kd of 1.44 nM and Bmax of 0.20 mol of [3H]SK&F-107260/mol of alpha v beta

36 ng scans yielded a Kd estimate of 3.4 nM and Bmax of 125-350 nM, in good agreement with the in vitro

37 nnexin II receptors with a Kd of 5.79 nm and Bmax of 2.13 x 10(5) receptors/cell.

38 in plasma membranes with a Kd = 69.6 pM and Bmax = 80 femtomoles/mg protein; no specific binding was

39 trend between the severity of vocal tics and Bmax values.

40 in a significant enhancement of the apparent Bmax for muscimol binding without significantly altering

41 d that phosphoramidon decreased the apparent Bmax from 7.3 to 5.8 fmol/mg protein.

42 d value of 0.3 +/- 0.2 nM and an approximate Bmax value of 1300 +/- 200 fmol/mg of protein.

43 l-3-iodoaminophenethyl-1-propylxanthine) are Bmax = 2-5 pmol/mg of protein and K(D) = 0.53 +/- 0.12 n

44 n), and down-regulation of cardiac beta-ARs (Bmax: knockout, 23 +/- 1 fmol/mg protein; WT, 31 +/- 2 f

45 T-PCR and 125I-labeled Ang II binding assay (Bmax, 2.21 and 1.19 fmol/mg protein, respectively).

46 blot, and 125I-labeled ox-LDL binding assay (Bmax, 29.7 ng/mg protein).

47 ume (DVstr) and DA D2 receptor availability (Bmax/Kd), for the placebo condition were similar for the

48 meter for dopamine transporter availability (Bmax/Kd + 1).

49 The average Bmax values for the same tissue preparations were 7.3 +/

50 Maximal ACE binding (Bmax) was 578+/-47 fmol/mg in IDC left ventricle (LV), 7

51 tely 2.5-fold increase in [(3)H]CFT binding (Bmax).

52 Maximum 125I-Ang II (125I-Ang II) binding (Bmax) was increased in LP rats (control n = 9, 291.6 +/-

53 tion constant of 130 pM and maximum binding (Bmax) of 240.0 fmol/mg protein.

54 Kd) = 54 pM and maximal theoretical binding (Bmax) = 13 fmol/mg protein), and inhibited by guanosine-

55 ation of konBmax and binding potential (BP = Bmax/Kd) and the reproducibility of the measures assesse

56 ysis [LEGA]), using binding potential (BPF = Bmax/Kd) (Bmax = maximum number of binding sites; Kd = d

57 to estimate 5-HT1A binding potential (BPF = Bmax/KD, where Bmax = available receptors and KD = disso

58 ding affinity for noncrosslinked fibrin, but Bmax was increased in the presence of ultrasound, from 3

59 55 +/- 0.93 nM and maximal binding capacity (Bmax) = 512.8 +/- 34.8 fmol/mg membrane protein.

60 02 nmol/L), with a maximum binding capacity (Bmax) of 414 fmol/10(6) cells (2.5 x 10(5) GRP-R/cell).

61 The maximum binding capacity (Bmax) of the high-affinity radioligand [3H]PN200-110 in

62 l protein, with the ligand-binding capacity (Bmax) typically 20-fold higher than that obtained with r

63 inity (Kd = 6 nM); maximum binding capacity (Bmax) was 275 fmol/mg protein.

64 Kd, 4.23 nM, and saturable binding capacity (Bmax), 6.38 pmol/mg protein.

65 gh affinity (Kd=5.2nM) and limited capacity (Bmax of 14.2fmol/mg of protein), confirming the presence

66 cell membrane proteins (deglycosylated cells Bmax: 6.83 Hz; glycosylated cells Bmax: 7.35 Hz).

67 ated cells Bmax: 6.83 Hz; glycosylated cells Bmax: 7.35 Hz).

68 urable using SK-N-MC neuroepithelioma cells (Bmax, 4.28 x 10(7) molecules of chelator/cell; and Kd, 2

69 nificantly increased the Kd without changing Bmax of [3H]CGP-39653 binding.

70 estimate the in vivo receptor concentration (Bmax) and dissociation equilibrium constant (Kd).

71 In contrast, Bmax in the allopurinol treated asphyxia group was simil

72 f a high level of CB1 receptors in controls (Bmax=12.0+/-0.3 pmol mg-1 protein) which decreased signi

73 In the cortex, Bmax was not affected in morphine tolerant or dependent

74 glycine binding sites increased at 45 days (Bmax:392 +/- 30 vs. 561 +/- 96 fmol/mg protein, P < 0.00

75 rotein, P < 0.005) but decreased at 60 days (Bmax:583 +/- 85 vs. 411 +/- 65 fmol/mg protein, P < 0.00

76 eatment with RC-3095 significantly decreased Bmax of receptors for EGF.

77 found to be 15.3 pM (KD) and 81.02m degrees (Bmax) with probe 1 and 54.9pM and 55.29m degrees (Bmax),

78 with probe 1 and 54.9pM and 55.29m degrees (Bmax), respectively.

79 istant inhibition of SERT binding densities (Bmax).

80 The densities (Bmax) of A1-AdoRs were 5.8 +/- 0.8 fmol/mg protein in 6-

81 ed to measure the affinity (Kd) and density (Bmax) of kainate and AMPA receptors in striatum, cortex

82 namely, by regulating the apparent density (Bmax) of GABAB receptors.

83 ith DPDPE for 2 or 4 days decreased density (Bmax) of [3H]DPDPE to bind to brain homogenates by 77 an

84 bably the result of a loss of nAChR density (Bmax ) and changes in the subunit composition of nAChRs.

85 is due to a change in the receptor density (Bmax) and/or affinity (measured as Kd) of the mu (mu) an

86 Receptor density (Bmax) in the striata of clinically stable spf/Y mice and

87 The receptor density (Bmax) in the untreated asphyxia group was decreased comp

88 Although 5-HT2A receptor density (Bmax) in the uterine artery was not changed in chronical

89 ide an absolute measure of receptor density (Bmax).

90 The authors determined the density (Bmax) and affinity (Kd) of platelet membrane 5-HT2A rece

91 The density (Bmax) of the high-affinity sites was significantly eleva

92 measures obtained were V3 (receptor density [Bmax]/equilibrium dissociation constant [KD]), V3' (f1 x

93 A Scatchard plot was used to estimate Bmax, and Kd(ND) = Kd/fND, the Kd value with respect to

94 Estimated Bmax ranged from 0.3 to 6.1 nM across ROIs and animals.

95 the first (E1) and second (E2) evaluations (Bmax/Kd, E1: 2.77+/-0.44; E2: 2.97+/-0.44).

96 cDNAs resulted in high levels of expression (Bmax = 95 +/- 6 pmol/mg) of the C-His-TxA2 receptors.

97 alculation of receptor availability ([3H]FMZ Bmax).

98 [3H]FMZ Bmax, determined autoradiographically from the same hipp

99 iazepine receptor concentration ([(11) C]FMZ Bmax) revealed significant intergroup differences in the

100 e of applying a more quantitative method for Bmax determination to PET imaging analysis.

101 CPP had no effect on [3H]glutamate Bmax or Kd during normoxia.

102 another lower affinity KD and another higher Bmax, but for ReLPS, LBP increased the affinity of bindi

103 In antidepressant-treated suicides however, Bmax values were lower in all regions, reaching statisti

104 MP-induced changes in striatal DV and in Bmax/Kd, as well as the behavioral and cardiovascular ef

105 tagonist) revealed no age-related changes in Bmax for either the mu or delta-opioid receptors.

106 eric agonists detects significant changes in Bmax values with little change in Kd, suggesting a G pro

107 in and hippocampus and was due to changes in Bmax values.

108 PERFIT pretreatment was due to a decrease in Bmax with no change in Kd.

109 ive as indicated by a shift in Kd but not in Bmax.

110 In the frontal cortex, the reduction in Bmax values was significantly greater in 3 months vs. 22

111 The dose-dependent reduction in Bmax was accompanied by a concentration-related decrease

112 to 343 nmol/L (P = .026) and also increased Bmax from 22 mumol/L to 25 mumol/L (P = .015).

113 activation was associated with an increased Bmax and unchanged Ki for [3H]WIN 35,428.

114 an up-regulation of mu-receptors (increased Bmax) in the striatum of rats treated with 0.3 mg/kg nic

115 the KD to 4.8 nM but only slightly increased Bmax to a maximum of 0.61 mol/mol-subunit.

116 e number of glycine binding sites increased (Bmax:392 +/- 30 vs. 583 +/- 30 fmol/mg protein at 45 and

117 ]), using binding potential (BPF = Bmax/Kd) (Bmax = maximum number of binding sites; Kd = dissociatio

118 WT (Bmax = 52 fmol/mg protein) and beta3 KO (Bmax = 53 fmol/mg protein) mice.

119 nogen (HK) (apparent Kd of 23 +/- 11 nmol/L, Bmax of 1.7 +/- 0.5 x 10(7) sites per cell [mean +/- SD,

120 scovery process, involving expression level (Bmax) and biodistribution determination, a PET-specific

121 nishment and anger had a significantly lower Bmax.

122 nstant (K(d)) of 4.4 nM and binding maximum (Bmax) 9.8 pmol/mg.

123 more numerous in the cocaine users: the mean Bmax value was 9.0 fmol bound/microg protein (SD = 2.8)

124 antly reduced in chronic EtOH exposed mouse (Bmax = 7.58 +/- 0.22 for control; 6.42 +/- 0.20 pmol/mg

125 ceptor exhibited high (Kd = 0.4 +/- 0.08 nM, Bmax = 0.7 +/- 0.2 pmol/mg protein; n = 4) and low (Kd =

126 nity to the P2X4 purinoceptor (KD = 0.13 nM, Bmax = 151 pmol/mg of protein).

127 3157 sites) and low affinity (K(d) = 157 nM, Bmax = 204,948 sites) elements.

128 tochondria with high affinity (Kd = 0.34 nM, Bmax = 80 fmol/mg of mitochondrial protein).

129 sic curve with high affinity (K(d) = 1.4 nM, Bmax = 3157 sites) and low affinity (K(d) = 157 nM, Bmax

130 rotein; n = 4) and low (Kd = 75 +/- 27.4 nM, Bmax = 7.1 +/- 3.6 pmol/mg protein; n = 4) affinity for

131 owed a high-affinity binding (Kd = 15.71 nM, Bmax = 1930 fmol/mg protein).

132 howed a high-affinity binding (Kd = 5.80 nM, Bmax = 1800 fmol/mg protein).

133 ed platelets (Kd app of approximately 10 nm; Bmax of approximately 1,500 sites/platelet) utilizing re

134 microM without altering the maximum number (Bmax) of [3H]ryanodine-binding sites.

135 The number (Bmax) of strychnine-sensitive glycine receptors (GlyR) d

136 EB did not change the number (Bmax) or affinity (Kd) of CCK receptors in the NTS.

137 ) and lowered the maximal binding occupancy (Bmax).

138 03545 permitted the successful estimation of Bmax and Kd(ND) in vivo.

139 Measurements of Bmax (number of functional receptors) and Kd (apparent r

140 orphin II) indicated no effect of ethanol on Bmax or Kd in striatum.

141 ant effects on the Kd 244 nmol/L site nor on Bmax.

142 ble and of high affinity (KD = 74 +/- 14 PM, Bmax = 679 +/- 88 fmol/mg protein; three experiments).

143 Mu-opioid receptor binding potential (Bmax/Kd) was found to increase with age in neocortical a

144 asure proportional to the binding potential (Bmax/KD), was derived.

145 , kinetic analysis of the binding potential [Bmax/(Kd x Vd)] using the assumption of equal partition

146 d alpha1B-adrenoceptor density ([3H]prazosin Bmax) versus control groups by 12% (1 microM AO) and 72%

147 There was an up-regulation of mu-receptor (Bmax increased) in the spinal cord of morphine tolerant

148 induced decrease in the number of receptors (Bmax) and receptor binding affinity (Kd) during hypoxia.

149 high affinity binding sites, with a reduced Bmax.

150 ibition constant (Ki) of 6.3 nM and regional Bmax in humans.

151 e in IPL was rapid (T1/2 15 min), saturable (Bmax appr.

152 Binding was saturable (Bmax = 12.6 pmol/mg of protein) and reversible.

153 [3H]-(-)-Trans-H2-PAT binds saturably (Bmax approximately 13 fmol/mg protein) and with high aff

154 However, the two-PET scan Bmax measurement demonstrated that 4 of the 20 patients

155 GC-C and GC-CD853A showed similar Bmax and Kd values for [125I]STa binding in these cells,

156 0 to 5.5 nM, and the number of binding sites Bmax ranged from 630 to 1360 molecules of C1q per bacter

157 9.8 nM and maximal density of binding sites (Bmax) = 42.4 fmol/mg of protein.

158 platelet tritiated paroxetine binding sites (Bmax) and dissociation constant (Kd) values were measure

159 The maximum number of binding sites (Bmax) estimated using [125I]L-750,667 in hD4 HEK cells w

160 constant (Kd) and the maximum binding sites (Bmax) in a bovine membrane preparation and similar rabbi

161 he maximum number of receptor binding sites (Bmax) values were derived from baseline VT and from the

162 imum density of [3H]PN200-110 binding sites (Bmax) was reduced approximately 3.9-fold.

163 The total number of binding sites (Bmax) was reduced significantly in bronchi and parenchym

164 ficity, and maximum number of binding sites (Bmax) were quantified, with adenoviral-expressed CXCR4 o

165 arly exclusively to a single class of sites (Bmax, 52 +/- 12 microg/mg; Kd, 150 +/- 28 nM).

166 creased the number of 5-HT1A receptor sites (Bmax = 108 +/- 8.20 fmol/mg protein and 152.31 +/- 13.36

167 increasing the density of recognition sites (Bmax).

168 aturable (maximal density of receptor sites, Bmax = 1.56 pmol (mg protein)-1) binding site that exhib

169 face area of HV, surface area of T1Gd, and T/Bmax.

170 /Bs greater than 1.2, and the maximum T/B (T/Bmax) was determined by the voxel with the greatest T/B

171 and MRI regions; the magnitude of hypoxia, T/Bmax, remains independent of size.

172 The T/Bmax, typically located within the T1Gd region, was inde

173 The Bmax establishes one [3H]AzTHP binding site per FAD.

174 The Bmax findings in the subgroup do not exclude an effect o

175 The Bmax for activated alpha2M was increased from 56 +/- 5 t

176 The Bmax for beta-carotene binding to the high affinity site

177 The Bmax in homogenates of these three regions in young cont

178 The Bmax, but not Kd, values of platelet tritiated paroxetin

179 [3H]diprenorphine was 1.1+/-0.2 nM, and the Bmax was 2.6+/-0.4 pmol/mg.

180 for human VAChT was 4.1 +/- 0.5 nM, and the Bmax was 8.9 +/- 0.6 pmol/mg.

181 ing revealed that hypoxia decreased both the Bmax and the Kd of the NMDA receptor for [3H]glutamate a

182 analyses showed that HTG-VLDL decreased the Bmax for 125I-labeled Glu-Pmg ligand binding approximate

183 Digestion decreased the Bmax for binding and the Vmax for uptake in amounts that

184 s treatment with deltorphin II decreased the Bmax of [3H]DPDPE by 76 and 87%, respectively.

185 h an IC50 value of 0.5 microM, decreased the Bmax value of the binding sites with a slight increase i

186 We conclude that hypoxia decreases the Bmax and Kd of the NMDA receptor glutamate recognition s

187 d that there was no alteration in either the Bmax or Kd for this ligand, suggesting that the changes

188 it from the transfection affected either the Bmax or the apparent KD of the receptor.

189 In hippocampus, the Bmax of [3H]MK-801 was increased but the Kd was decrease

190 TH was also found to cause a decrease in the Bmax for [3H]raclopride binding, suggesting that persist

191 inity binding site and a 27% increase in the Bmax of the low affinity binding site.

192 Second, differences in the Bmax value of agonist-stimulated [35S]GTP gamma S bindin

193 hr resulted in a significant decrease in the Bmax value of opioid receptors, with a maximum reduction

194 , the changes were due to alterations in the Bmax values.

195 M EEDQ for 1 h caused a 40% decrease in the Bmax, without changing the K(d).

196 KD and only about a 2-fold reduction in the Bmax.

197 necessity of estrogen priming, increased the Bmax of baclofen binding to GABAB receptors in the neoco

198 EEIIMD increased the Bmax of scuPA binding 4-fold with the half-maximal effec

199 ith (+)-pentazocine or PRE-084 increased the Bmax values of [(3)H]WIN35428 binding to DAT in rat stri

200 Cl- concentration altered the Kd but not the Bmax of binding.

201 by approximately 95%, and Y898R reduced the Bmax and ATPase activity by approximately 60%.

202 Q mutation in Na,K-ATPase alpha3 reduced the Bmax for ouabain binding and the ATPase activity of alph

203 , or 3.0 microM FSCPX for 30 min reduced the Bmax of [3H]CPX binding by 41 +/- 10%, 67 +/- 6%, and 80

204 S]GTP gamma S binding in SPM showed that the Bmax of cannabinoid stimulated binding was significantly

205 - 71 fmol/mg, which correlated well with the Bmax value determined using [3H]spiperone (227 +/- 83 fm

206 This Bmax measure also revealed a significant (p < 0.05) asso

207 ing potential (BP) (which is proportional to Bmax/KD, in which Bmax is transporter density and KD is

208 The turnover (Vmax/Bmax) of the human VAChT was approximately 65/min.

209 HT1A binding potential (BPF = Bmax/KD, where Bmax = available receptors and KD = dissociation constan

210 strained to be constant across ROIs, whereas Bmax was allowed to be ROI-dependent and animal-dependen

211 (which is proportional to Bmax/KD, in which Bmax is transporter density and KD is dissociation const

212 icular membranes from the hearts of both WT (Bmax = 52 fmol/mg protein) and beta3 KO (Bmax = 53 fmol/

213 brium dissociation constant [KD]), V3' (f1 x Bmax/KD), and RT (specific-to-nondisplaceable tissue rat

214 on analysis of [3H]ryanodine binding yielded Bmax = 150 fmol/mg of protein and Kd = 110 nM in DAKIKI

215 ioligand 125I-labeled AB-MECA, which yielded Bmax and Kd values of 1.31 pmol/mg protein and 3.19 nmol

216 rafts was assessed by Western blot, yielding Bmax/Kd = 14.

217 the A2A selective antagonist, 125I-ZM241385 (Bmax=843 receptors/neutrophil; KD=0.125 nM).