997 resultados para ddc:621.3


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Ca2+-sensitivity of sheep lung cyclic-3',5'-nucleotide phosphodiesterase is provided by endogenous tightly bound calmodulin. The calcium sensitivity of a highly purified enzyme was desensitized by increasing the assay temperature. It could also be desensitized to Ca2+-activation by thiols such as dithiothreitol. The thiol-induced desensitization could be partially reversed by dialysis and almost completely reversed by dilution. The results presented in this paper indicate that thiols are possibly involved in the interaction of calmodulin with cyclic-3',5'-nucleotide phosphodiesterase. This is the first report on temperature and thiol-induced desensitization of Ca2+-sensitivity of a cyclic-3',5'-nucleotide phosphodiesterase.

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C22H31NO2.H2 O, M r = 359" 5, orthorhombic,P2~212 ~, a= 10.032 (1), b= 11.186 (1), C = 17.980 (1)/~,, U= 2017.48/~3, Z = 4, D x = 1.276 Mg m -a, 2(Cu Kct) = 1.5418/~, # = 0.69 mm -~,F(000) = 784, T = 293 K. Final R = 0.05 for 1972 unique reflections with I > 3o(/). Ring A is planar, and rings B and C adopt a chair conformation. Rings D and E are envelopes, with C(14) and C(20) displaced from their respective ring planes by 0-616 (2) and 0.648 (3)/~. The A/B ring junction is quasi-trans,whilst ring systems B/C and C/D are trans fused about the bonds C(8)-C(9) and C(13)-C(14) respectively.The D/E junction shows cis fusion.

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Abstract. C25H44N20 , M r= 388.6, orthorhombic, P21212 I, a = 6.185 (2), b = 18.123 (2), c = 20.852 (2) A, U= 2337.2 A 3, Z = 4, D x = 1.104 Mg m -a, 2(Cu Ka) = 1.5418 A,/~ = 0.47 mm -~, F(000) = 864, T= 293 K. Final R - 0.038 for 1791 reflections with I >_ 3a(I). Rings A and C are in chair conformation. Ring B is in an 8fl,9a-half-chair conformation. Ring D adopts a conformation in between 13fl,14a-half-chair and 13t-envelope. There is a quasitrans fusion of rings A and B, whilst ring systems B/C and C/D are trans fused about the bonds C(8)-C(9)and C(13)-C(14).

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The enzymatic pathway for the synthesis of sn-glycerol 3-phosphate was investigated in developing groundnut seeds (Arachis hypogaea). Glycerol-3-phosphate dehydrogenase was not detected in this tissue but an active glycerokinase was demonstrated in the cytosolic fraction. It showed an optimum pH at 8.6 and positive cooperative interactions with both glycerol and ATP. Triosephosphate isomerase and glyceraldehyde-3-phosphate phosphatase were observed mainly in the cytosolic fraction while an active glyceraldehyde reductase was found mainly in the mitochondrial and microsomal fractions. The glyceraldehyde 3-phosphate phosphatase showed specificity and positive cooperativity with respect to glyceraldehyde 3-phosphate. The glyceraldehyde reductase was active toward glucose and fructose but not toward formaldehyde and showed absolute specificity toward NADPH. It is concluded that in the developing groundnut seed, sn-glycerol 3-phosphate is synthesized essentially by the pathway dihydroxyacetone phosphate ? glyceraldehyde 3-phosphate ?Pi glyceraldehyde ?NADPH glycerol ?ATP glycerol 3-phosphate. All the enyzmes of this pathway showed activity profiles commensurate with their participation in triacylglycerol synthesis which is maximal during the period 15�35 days after fertilization. Glycerokinase appears to be the rate-limiting enzyme in this pathway.

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The e.m.f. of a concentration cell for SO x (x=2,3)-O2 incorporating Nasicon as the main solid electrolyte has been measured in the temperature range 720 to 1080 K. The cell arrangement can be represented as,$$Pt, O'_2 + SO'_2 + SO'_3 \left| {Na_2 SO_4 \left\| {\left. {Nasicon} \right\|} \right.} \right.\left. {Na_2 SO_4 } \right|SO''_3 + SO''_2 + O''_2 , Pt$$ The Na2SO4 acts both as an auxiliary electrode, converting chemical potentials of SO x and O2 to equivalent sodium potentials, and as an electrolyte. The presence of Na2SO4 provides partial protection of Nasicon from chemical reaction with gas mixtures containing SO x . The open circuit e.m.f. of the cell is in close agreement with values given by the Nernst equation. For certain fixed inlet gas compositions of SO2+O2, the e.m.f. varies non-linearly with temperature. The intrinsic response time of the cell to step changes in gas composition is estimated to vary from sim2.0 ksec at 723K to sim 0.2 ksec at 1077K. The cell functions well for large differences in partial pressures of SO3(pPrimeSO 3/pprimeSO 3ap104) at the electrodes.