ライフサイエンスコーパス: tripolyphosphate

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1 anganese and are inept at cleaving inorganic tripolyphosphate.

2 0.05% and 3% sodium trimetaphosphate/sodium tripolyphosphate.

3 tive inhibitors of cvRtp1 (K(i) = 0.6 microm tripolyphosphate and 2.4 microm pyrophosphate, respectiv

4 ociated to the presence of adulterants NaCl, tripolyphosphate and carrageenan.

5 We found that tripolyphosphate and pyrophosphate were potent competiti

6 = 13), demonstrated that Zn, orthophosphate, tripolyphosphate, and hexametaphosphate corrosion/scalin

7 ated with Fo and GDP, GTP, pyrophosphate, or tripolyphosphate, and the hydrolysis of F(420)-0 to Fo.

8 anisms of AdoMet formation and hydrolysis of tripolyphosphate are proposed.

9 o AdoMet, PP(i), and P(i), with formation of tripolyphosphate as a tightly bound intermediate.

10 he sulfur of methionine displaces the intact tripolyphosphate chain (PPP(i)) from ATP, and subsequent

11 P = Mg(2+); and for myosin V pyrophosphate = tripolyphosphate > ATP-Mg(2+) = ATP = AMP-PNP > ADP = te

12 adenylyl imidodiphosphate) > pyrophosphate = tripolyphosphate > tetrapolyphosphate = ADP > cAMP = Mg(

13 5*A enzyme has a 100-fold greater k(cat) for tripolyphosphate hydrolysis than the wild type enzyme, b

14 alytic impairment in the partial reaction of tripolyphosphate hydrolysis.

15 = 1 mM), pyrophosphate (I(0.5) = 0.4 mM) and tripolyphosphate (I(0.5) = 30 microM).

16 0-fold whereas the rate of hydrolysis of the tripolyphosphate intermediate is decreased by less than

17 We show that tripolyphosphate is a potent competitive inhibitor of Tb

18 substrate for AdoMet formation during which tripolyphosphate is produced.

19 le to those obtained from tetrapolyphosphate-tripolyphosphate mixtures.

20 m oil and beta-carotene with chitosan/sodium tripolyphosphate or chitosan/carboxymethylcellulose and

21 d from tetrapolyphosphate in the presence of tripolyphosphate or NH4NO3 at higher concentrations (app

22 r diphosphates but not AMP, cAMP, adenosine, tripolyphosphate, or pyrophosphate.

23 rsion steps [AdoMet formation and subsequent tripolyphosphate (PPP(i)) hydrolysis], and product relea

24 describes a nonhydrolyzable analogue of the tripolyphosphate (PPP(i)) reaction intermediate, diimido

25 hetase catalyzes the formation of AdoMet and tripolyphosphate (PPPi) from ATP and L-methionine and th

26 rase) catalyzes a two-step reaction in which tripolyphosphate (PPPi) is a tightly bound intermediate.

27 enzyme, EutT was not inhibited by inorganic tripolyphosphate (PPPi).

28 f the methionine segment of AdoMet or in the tripolyphosphate segment of AMPPNP, these portions of th

29 low stripe trevally surimi added with sodium tripolyphosphate (STPP) (0.25% and 0.5%, w/w) and protei

30 rn leatherjacket, phosphorylated with sodium tripolyphosphate (STPP) at various concentrations (0.25%

31 zed by their ability to hydrolyze a range of tripolyphosphate substrates.

32 ) CthTTM is 150-fold more active in cleaving tripolyphosphate than ATP and (ii) the substrate specifi

33 ATP and l-methionine (Met) and hydrolysis of tripolyphosphate to PP(i) and P(i).

34 ur of bovine serum albumin (BSA) in chitosan-tripolyphosphate (TPP) hydrogel beads.

35 Chitosan (CH)-tripolyphosphate (TPP) submicron particles were formed a

36 NPs) prepared by ionic gelation with sodium tripolyphosphate (TPP), further encapsulated in ZN micro

37 lyphosphates [orthophosphate, pyrophosphate, tripolyphosphate, trimetaphosphate, and tetrapolyphospha

38 f microparticles coated with chitosan/sodium tripolyphosphate was approximately 55%, while that of mi

39 cts of increased fat content and addition of tripolyphosphate were observed.

40 ysis of all dNTPs to the deoxynucleoside and tripolyphosphate, which effectively depletes the dNTP su

41 ed by ionic gelation of chitosan with sodium tripolyphosphate, which presented a spherical morphology

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