ライフサイエンスコーパス: oxygen affinity

1 anion binding site could result in increased oxygen affinity.

2 ses the hypothermia-dependent increase in Hb oxygen affinity.

3 reas alpha+M exhibits a significantly higher oxygen affinity.

4 emoprotein, named cyanoglobin, that has high oxygen affinity.

5 asparagine in an attempt to engineer higher oxygen affinity.

6 s, despite greater than 40-fold increases in oxygen affinity.

7 maintain cooperativity, but possess lowered oxygen affinity.

8 d haemolysis, an effect not due to increased oxygen affinity.

9 thus reduce sulfhydryl reactivity as well as oxygen affinity.

10 blood cell (RBC) sickling is to increase HbS oxygen affinity.

11 rm and that dissociation would lead to lower oxygen affinity.

12 mal hemoglobin and DecHb have a very similar oxygen affinity.

13 ed dynamics has been associated with lowered oxygen affinity.

14 tion in the full-length enzyme did not alter oxygen affinity.

15 oes not show an inverse correlation with the oxygen affinity.

16 olecular modification, molecular volume, and oxygen affinity.

17 HP causing a more pronounced decrease in its oxygen affinity.

18 viously studied rHb(alphaL29F) exhibits high oxygen affinity.

19 oglobin Jamaica Plain," had severely reduced oxygen affinity.

20 state, along with a significant increase in oxygen affinity.

21 cs of reduction are directly proportional to oxygen affinity.

22 the modification and restored the predicted oxygen affinity.

23 and two hemoglobin solutions with different oxygen affinities.

24 ssessment of measures of fetal and placental oxygen affinities.

25 inant hemoglobin had significantly different oxygen affinities.

26 igand, which accounts for its unusually high oxygen affinity (222 microm(-1)).

27 synthetic allosteric modifier of hemoglobin-oxygen affinity, a 2-[4-[[(3,5-disubstituted anilino)car

28 ies of cell-free Hb, including cost, overall oxygen affinity, alterations in cooperativity, and ready

29 lpha V96W, beta N108K), which has the lowest oxygen affinity among the hemoglobins studied, has the g

30 n leads to approximately 3-fold increases in oxygen affinity and 4-6-fold decreases in CO affinity.

31 s 50% saturated (P50 ) is a measure of blood oxygen affinity and a gauge of the tolerance of animals

32 This results in an 8-fold increase in oxygen affinity and a marked decrease in cooperativity.

33 beta 1 subunit interface can affect both the oxygen affinity and cooperativity of the oxygenation pro

34 unpolymerized sickle hemoglobin (HbS), whose oxygen affinity and cooperativity profile are equal to t

35 of the heme group, and substantially reduces oxygen affinity and cooperativity.

36 en binding experiments reveal an increase in oxygen affinity and decrease in cooperativity as the con

37 in response to S-nitrosation, with increased oxygen affinity and decreased cooperativity.

38 ickle cell disease (SCD), thereby increasing oxygen affinity and decreasing HbS polymerization and RB

39 The dual activities of increasing HbS oxygen affinity and directly inhibiting deoxy HbS polyme

40 lphaV96W, betaN108K), but still exhibits low oxygen affinity and good cooperativity.

41 rHb(alphaV96W, betaN108K) exhibits low oxygen affinity and high cooperativity and also ease of

42 t hemoglobins (rHbs) with moderately lowered oxygen affinity and high cooperativity compared to human

43 tructure, we will have a hemoglobin with low oxygen affinity and high cooperativity.

44 important functional properties, such as low oxygen affinity and high cooperativity.

45 uced such a mutation into our rHb having low oxygen affinity and high cooperativity.

46 arate; the modified hemoglobin has increased oxygen affinity and lacks cooperativity.

47 b(beta L105W) does indeed possess a very low oxygen affinity and maintains normal cooperativity (P(50

48 he monomeric hemoglobins with relatively low oxygen affinity and one monomeric hemoglobin of intermed

49 both binding sites, there are differences in oxygen affinity and oxyferrous state lifetime that may b

50 They differ from each other only in oxygen affinity and oxygen dissociation rate constants,

51 tramolecular disulfide bond that affects its oxygen affinity and protein stability.

52 The increased oxygen affinity and R-state character that result from S

53 etaL28F), and rHb(betaL28W) exhibit very low oxygen affinity and reduced cooperativity compared to th

54 of C-terminal residues in hemoglobin raises oxygen affinity and reduces both cooperativity and the B

55 meric structure of hemoglobin and its normal oxygen affinity and vasoactivity.

56 ccurring abnormal human hemoglobin with high oxygen affinity and very low cooperativity, are quite di

57 pentacoordinate ferrous heme iron, moderate oxygen affinity, and a relatively rapid oxygen dissociat

58 ned in a reduced state, necessary for normal oxygen affinity, and incapable of oxygen-linked NO stora

59 ibits increased anion sensitivity, increased oxygen affinity, and increased ease of oxidation, but wi

60 globin with a hexacoordinate heme iron, high oxygen affinity, and slow oxygen dissociation rate const

61 Oxygen affinity, as measured by P(50), did not respond t

62 esence of a transition between two different oxygen affinities at the beginning and end of the isothe

63 ared to rHb (beta N108Q), but exhibits lower oxygen affinity at pH below 7.4 and good cooperativity a

64 tribute to adaptive differentiation in blood-oxygen affinity between high- and low-altitude populatio

65 a large and significant part of the shift in oxygen affinity brought about by anion binding occurs as

66 the first PAS domain strongly increased the oxygen affinity but essentially prohibited autophosphory

67 bin are too low to affect overall hemoglobin oxygen affinity, but augmented NO transport to the micro

68 al human hemoglobin variant that has lowered oxygen affinity, but unaltered cooperativity and anion s

69 trength and if changes in fetal or placental oxygen affinities can be detected in time to allow for e

70 modifications are introduced that lower the oxygen affinity, can limit the safety of these proteins.

71 While R state haemoglobin has an oxygen affinity close to that of isolated subunits, the

72 ately 10(-)3 Torr) while Hb Lucina II has an oxygen affinity comparable to that of Mb (P50 = 0.13 Tor

73 ess, conversion of this Tyr to Phe increases oxygen affinity considerably, suggesting that hydrogen b

74 The increase in SS RBC oxygen affinity correlated with the NO concentration.

75 In contrast to the very high oxygen affinities displayed by most hexacoordinate hemog

76 that greater mass in the heme pocket lowers oxygen affinity due to impaired movement of the heme iro

77 The decrease in oxygen affinities for Hb F gammaG1V, gammaS143H with inc

78 d that there are several regions of enhanced oxygen affinity for the protein both on the surface and

79 oxygenated T-state tetramer to assume higher oxygen affinity forms (T', T", T"'...) with less steric

80 previously reported), Val, and Tyr increases oxygen affinity from 8- to 100-fold over that of the wil

81 the engineered Trp residue, and the lowered oxygen affinity had been attributed to a stabilization o

82 Membrane modulation of hemoglobin oxygen affinity has particularly interesting implication

83 -phospho propylation first to generate a low oxygen affinity Hb, HPPr-HbA.

84 On the basis of its low oxygen affinity, high cooperativity, and stability again

85 rHb (beta N108Q) exhibits low oxygen affinity, high cooperativity, enhanced Bohr effec

86 Tuna species display a wide range of blood oxygen affinities (i.e., P50 values) and therefore may b

87 gest that RSR13-BC, by decreasing hemoglobin oxygen affinity, improves oxidative metabolism and prese

88 Increased osmotic pressure, which lowers the oxygen affinity in human hemoglobin, raises the oxygen a

89 Thus, high oxygen affinity in leghemoglobin is established by a fav

90 e that the cross-link introducing the lowest oxygen affinity in the two singly cross-linked species a

91 en side chain packing in the heme pocket and oxygen affinity, indicating that greater mass in the hem

92 of distinct hemoglobin isoforms with graded oxygen affinities is expected to broaden the permissible

93 loride normal cooperativity is restored, and oxygen affinity is further lowered because the shape of

94 as compared to Hb A, suggesting that higher oxygen affinity is likely to be determined by the heme p

95 lain the fact that no comparable reversal of oxygen affinity is observed under identical conditions.

96 ture therapies, particularly those where the oxygen affinity is perturbed.

97 In addition, single-cell oxygen affinity is positively correlated with Hb concent

98 xplain why Hb Ascaris has one of the highest oxygen affinities known (P50 approximately 10(-)3 Torr)

99 d Hb Felix) retains cooperativity and has an oxygen affinity like that of HbA both in the presence an

100 variants at the beta93 position show higher oxygen affinity, lower cooperativity, and reduced Bohr e

101 The presence of 0.9 g/dL of high oxygen affinity MalPEG-Hb improves microvascular blood f

102 synthetic allosteric reduction in hemoglobin-oxygen affinity may be a new and important therapeutic s

103 Functional characterization included oxygen affinity measurements, CO combination rates, and

104 The rationale was that the high oxygen affinity MHOAH Hb, the lower oxygen affinity of H

105 gesting that hydrogen bonding is involved in oxygen affinity modulation.

106 n of Thr-72-->Val in the interface increases oxygen affinity more than 40-fold with a surprising enha

107 ult recombinant hemoglobin (rHb A) and a low-oxygen-affinity mutant recombinant hemoglobin, rHb(alpha

108 In contrast, oxygen affinities of Hb F gammaG1V, gammaE5P, gammaS143H

109 The recombinant double mutant has an oxygen affinity of 10 mm Hg, which is identical to that

110 Although the oxygen affinity of blood is well-understood and routinel

111 The extremely high oxygen affinity of Ctb makes it unlikely to function as

112 The basis for the high oxygen affinity of cyanoglobin was investigated through

113 constraints that are responsible for the low oxygen affinity of deoxyhemoglobin.

114 We measured the oxygen affinity of each oxidase, using a highly sensitiv

115 Using the strong oxygen affinity of gadolinium, we design a model system

116 Oxygen affinity of Hb F gammaG1V, gammaS143H in the abse

117 the high oxygen affinity MHOAH Hb, the lower oxygen affinity of Hb S Antilles than Hb S (P50 approxim

118 To further modulate the oxygen affinity of Hb, the alpha alpha-fumaryl cross-bri

119 ing 5-hydroxymethyl-2-furfural, increase the oxygen affinity of hemoglobin (Hb) and strongly inhibit

120 minal 11-residue synthetic peptide lower the oxygen affinity of hemoglobin but effects on cooperativi

121 low serum erythropoietin (EPO) level, normal oxygen affinity of hemoglobin, and typically autosomal d

122 are primarily responsible for modulating the oxygen affinity of hemoglobin.

123 is physiologically relevant in lowering the oxygen affinity of heterodimeric sGC and, therefore, sta

124 ructural insights led to the hypothesis that oxygen affinity of lamprey hemoglobin is distally regula

125 anges in chloride concentration, whereas the oxygen affinity of r Hb Presbyterian exhibits a pronounc

126 The oxygen affinity of r Hb Yoshizuka is insensitive to chan

127 The oxygen affinity of R206A BjFixL (Kd approximately 350 mi

128 s of nitric oxide (NO) gas would augment the oxygen affinity of RBCs containing homozygous HbS (SS).

129 nds are the structural basis for the lowered oxygen affinity of rHb(alpha 96Val-->Trp), and discuss t

130 gen affinity in human hemoglobin, raises the oxygen affinity of Scapharca hemoglobin regardless of wh

131 inhalation has been reported to increase the oxygen affinity of sickle cell erythrocytes.

132 Thus, low concentrations of NO augment the oxygen affinity of sickle erythrocytes in vitro and in v

133 ge influence on the chemical composition and oxygen affinity of supported nanoparticles under X-ray i

134 explanation for the difference in hemoglobin oxygen affinity of the two quaternary structures.

135 alassemia have a significant decrease in the oxygen affinity of their hemoglobin, that is an increase

136 The oxygen affinity of these mutants is lower than that of h

137 e, indicating a possible reason for the high oxygen affinity of this derivative.

138 The oxygen affinity of this Hb is insensitive to DPG and IHP

139 derstand the variability and determinants of oxygen affinity on a cellular level, we have developed a

140 ls that inhibit polymerization by increasing oxygen affinity, one of them (GBT440) also inhibits sick

141 The oxygen affinity (P(50) = 0.45 Torr) is similar to that o

142 ve cation exchange chromatography, exhibited oxygen affinity (P(50)) values of 14.5, 12.1, and 15.5 T

143 ecies binds oxygen cooperatively with a high oxygen affinity (P50 = 4.8 torr at pH 7.4).

144 were bred into MHOAH mice that express high oxygen affinity (P50 approximately 24.5 mm Hg) rather th

145 Des-alpha-Arg141 hemoglobin had a higher oxygen affinity (P50, 5.51 mm Hg; control, 19.94 mm Hg [

146 ized to have a central role in regulation of oxygen affinity, plays at most only a small role in dict

147 The oxygen affinity reflects the average of the rapidly equi

148 ansport is enabled by their remarkably lower oxygen affinity relative to human alpha chains.

149 67I) and rHb (betaV67F) exhibit low and high oxygen affinity, respectively.

150 Significant reduction in oxygen affinity resulting from interactions between hete

151 Increased oxygen affinity results from the absence of the Phe97 si

152 he Fe(2+) to the Fe(3+) state than other low-oxygen-affinity rHbs developed in our laboratory, e.g.,

153 rcuribenzoate, and our results show that low-oxygen-affinity rHbs have a more reactive beta93Cys than

154 ore, the cooperativity index and the overall oxygen affinity seem to be correlated to the positive en

155 gammaE5P, gammaS143H, which exhibit reduced oxygen affinity, should facilitate design of efficient a

156 th more rapid kinetics occurring in the high oxygen affinity state (i.e. modification of the Cysbeta-

157 ification of the Cysbeta-93) than in the low oxygen affinity state (i.e. treatment with inositol hexa

158 lay an important role in maintaining the low-oxygen-affinity state (T state) in deoxy HbA, but a late

159 These proteins often have very high oxygen affinities stemming from very slow ligand off rat

160 ral pH range according to the proton NMR and oxygen affinity studies presented here.

161 B- and C-families also have higher apparent oxygen affinities than the A-family.

162 e of the central cavity and exhibits a lower oxygen affinity than wild-type HbA in the presence of ch

163 HbAS3 binds oxygen cooperatively and has an oxygen affinity that is comparable with fetal hemoglobin

164 of synthetic peptide to Hb, resulting in an oxygen affinity that is moderately decreased and a parti

165 tion of the second cross-linking reduces the oxygen affinity to 15.9 torr, which compares with 13.0 t

166 Monomeric invertabrate hemoglobins with high oxygen affinity usually contain a tyrosine in the distal

167 icity in the distal heme pocket can decrease oxygen affinity via steric hindrance effects while incre

168 Convergent increases in hemoglobin-oxygen affinity were pervasive among high-altitude taxa,

169 al for viability and exhibited a much higher oxygen affinity, with a K(m) value of 40 nM and a V(max)