ライフサイエンスコーパス: pCMBS

1 pCMBS accessibility is (i) reduced when the transporter

2 pCMBS had no effect on either glucose transporter activi

3 pCMBS inactivated the wild-type P2Y(12) receptor in a co

4 pCMBS mildly inhibited mutants A739C, A740, V747C, and Q

5 pCMBS(-), applied with GABA, reacted with 14 of the 19 r

6 pCMBS- reacted with cysteines substituted at the four po

7 g agent p-chloromercuribenzenesulfonic acid (pCMBS) had no effect on 3H-FDG uptake under normoxic con

8 such as p-chloromercuribenzosulphonic acid (pCMBS), p-chloromercuribenzoate (pCMB), mersalyl acid an

9 o 0.5 mM p-chloromercuriphenylsulfonic acid (pCMBS), but this had no effect on rates of intracellular

10 agent p-chloromercuribenzene sulfonic acid (pCMBS) and the active metabolites from antiplatelet drug

11 ), and p-chloromercuribenzene sulfonic acid (pCMBS).

12 The inhibitors 4-CIN and pCMBS, but not quercetin, blocked lactate uptake by axon

13 ake was inhibited by phloretin (0.75 mM) and pCMBS (0.5 mM) (55 and 32% inhibition, respectively).

14 ntly reduces the apparent rate of beta2M286C-pCMBS bond formation, tracked electrophysiologically.

15 the cell membrane were minimally affected by pCMBS.

16 he R368C mutant channel was also affected by pCMBS.

17 Voltage dependence of block by pCMBS (2 min exposure) was steeper for L366C than for L3

18 x 3 single-cysteine mutants was inhibited by pCMBS, suggesting that only a small portion of this heli

19 steine mutants was demonstrably inhibited by pCMBS.

20 gly mutated V367C channel, were inhibited by pCMBS.

21 ed half activity, and both were inhibited by pCMBS.

22 tivities, and sensitivities to inhibition by pCMBS were determined.

23 titution at Leu(188) conferred inhibition by pCMBS, suggesting that most of helix 6 is not exposed to

24 functionally modified by negatively charged pCMBS(-).

25 ryl reagent p-chloromercuribenzenesulfonate (pCMBS(-)) applied extracellularly to cysteines substitut

26 ic reagent, p-chloromercuribenzenesulfonate (pCMBS(-)), by its effect on subsequent currents elicited

27 fication by p-chloromercuribenzenesulfonate (pCMBS) with and without GABA and tested if etomidate blo

28 ion rate of p-chloromercuribenzenesulfonate (pCMBS) with cysteines substituted in the GABA(A) recepto

29 ic reagent, p-chloromercuribenzenesulfonate (pCMBS).

30 ic reagent, p-chloromercuribenzenesulfonate (pCMBS).

31 ic reagent, p-chloromercuribenzenesulfonate (pCMBS).

32 ic reagent, p-chloromercuribenzenesulfonate (pCMBS).

33 ic reagent, p-chloromercuribenzenesulfonate (pCMBS).

34 ted reagent p-chloromercuribenzenesulfonate (pCMBS).

35 ic reagent, p-chloromercuribenzenesulfonate (pCMBS).

36 fic reagent p-chloromercuribenzenesulfonate (pCMBS-).

37 In the presence of 100 nM diazepam, pCMBS(-) reacted with alpha(1)F296C, alpha(1)F298C, and

38 e inhibited by incubation with extracellular pCMBS.

39 e inhibited by incubation with extracellular pCMBS.

40 Finally, pCMBS partially affected the G(i) coupling of Cys17Ser o

41 In the absence of diazepam or GABA, pCMBS(-) did not react at a measurable rate with cystein

42 Based on differences in pCMBS(-) reaction rates two domains can be distinguished

43 Positively (MTSEA(+)) and negatively (pCMBS(-)) charged sulfhydryl reagents, as well as Cd(2+)

44 d tested if etomidate blocks modification of pCMBS-accessible cysteines.

45 ited transport inhibition in the presence of pCMBS, and the extent of inhibition was minimal (11%), i

46 The subset of pCMBS(-)-accessible, M3 segment cysteine mutants acts as

47 at channel activation increases water and/or pCMBS access.

48 2-aminoethylmethane thiosulfonate (MTSEA) or pCMBS.

49 irectly activating concentration of propofol pCMBS(-) reacts with a different subset of the M3 cystei

50 e water-soluble, sulfhydryl-specific reagent pCMBS(-) was assayed electrophysiologically.

51 tivity and p-chloromercuribenzene sulfonate (pCMBS) accessibility of 21 cysteine-substituted NBC muta

52 ed reagent p-chloromercuribenzene sulfonate (pCMBS).

53 c reagent, p-chloromercuribenzene sulfonate (pCMBS).

54 c reagent, p-chloromercuribenzene-sulfonate (pCMBS).

55 es, using p-chloromercuribenzene sulphonate (pCMBS) as a probe.

56 Here we show that pCMBS(-), applied in the presence of a potentiating conc

57 The pCMBS(-) reaction rates with these three cysteine mutant

58 Additionally, the pCMBS data indicate that the predicted exoplasmic end of

59 2M2 segment 19' position, R269Q, altered the pCMBS reaction rate with several alpha1M1 Cys, some only

60 In the presence of GABA, the pCMBS reaction rate increased significantly in a cluster

61 The voltage dependence of the pCMBS effect was also shifted to more depolarising poten

62 We infer that the pCMBS(-) reactive residues are on the water-accessible s

63 s within helix 10 were clearly accessible to pCMBS as judged by inhibition or stimulation of transpor

64 ine 313, and glycine 314, were accessible to pCMBS as judged by the inhibition of transport activity.

65 embrane segment 5 were clearly accessible to pCMBS in the external medium, as determined by inhibitio

66 functional activities, and sensitivities to pCMBS were determined.

67 , transport activities, and sensitivities to pCMBS were determined.

68 , transport activities, and sensitivities to pCMBS were determined.

69 cose uptake activities, and sensitivities to pCMBS were determined.

70 yglucose uptake activity, and sensitivity to pCMBS were measured.

71 yglucose uptake activity, and sensitivity to pCMBS were measured.

72 e of the membrane resulted in sensitivity to pCMBS-induced transport inhibition.

73 receptor by site-directed mutagenesis using pCMBS as the thiol reagent.

74 beta(1)A252C (2') and beta(1)T256C (6') were pCMBS(-)-reactive in the presence of GABA.

75 In seven of eight residues where pCMBS modification was evident, rates of modification we

76 -), likely due to substrate competition with pCMBS; (ii) reduced in the presence of a stilbene inhibi

77 nd 365 (R362C and R365C) reacted faster with pCMBS than those in which cysteines were introduced in p

78 rmore, the R365C mutant channel reacted with pCMBS even at hyperpolarised (-120 mV) potentials.

79 1)Ala(291) and alpha(1)Tyr(294) reacted with pCMBS(-) applied both in the presence and in the absence

80 idues that we previously showed reacted with pCMBS(-) applied in the presence of GABA.

81 301), and alpha(1)Glu(303) only reacted with pCMBS(-) applied in the presence of GABA.

82 12') through beta(1)E270C (20') reacted with pCMBS(-) applied with GABA.

83 bstituted for beta2Met286 from reaction with pCMBS-.

84 -substitution mutants that are reactive with pCMBS(-) in the absence and presence of GABA and in the