The effect of pressure on the activity of ribonuclease

Williams, Rebecca S.; Shen, Chin

doi:10.1016/0003-9861(72)90256-1

Cited by 15 publications

(4 citation statements)

References 30 publications

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“…In this experiment, the virus was pressurized in the presence of ribonuclease. Ribonuclease activity is not affected in this pressure range (Williams & Shen, 1972), and the presence of the enzyme did not modify the dissociation curve (not shown). The RNA was not digested by ribonuclease under pressure, suggesting that coat proteins protect the RNA even in a partially unfolded state.…”

Section: Different States In the Dissociation Of Virusesmentioning

confidence: 71%

Partially folded states of the capsid protein of cowpea severe mosaic virus in the disassembly pathway

Gaspar

Johnson

Silva

et al. 1997

Journal of Molecular Biology

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Section: Different States In the Dissociation Of Virusesmentioning

confidence: 71%

Partially folded states of the capsid protein of cowpea severe mosaic virus in the disassembly pathway

Gaspar

Johnson

Silva

et al. 1997

Journal of Molecular Biology

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“…These two opposite factors seem to be involved in phosphate hydrolyzing enzyme reactions, in general. The reported pressure dependence of ribonuclease (Williams and Shen, 1972), 5'-nucleotidase (Penniston, 1971), plant endonucleases (Kunugi et af., 1989a) or cyclodextrin ribonuclease model reactions have shown positive apparent activation volumes derived from the second-order rate measure-ment; mostly the former (K,) contribution is dominant and deceleration by pressure was observed. The present results showing pressure dependence on K , and k,,, and the consequent apparent pressure insensitivity might be derived from small but even counteraction by these two factors.…”

Section: H Kabata E T a Lmentioning

confidence: 99%

Effect of high of pressure of EcoRI reactions

Kabata

Nomura

Shimamoto

et al. 1994

J of Molecular Recognition

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The effect of pressure on reactions of restriction endonucleases was investigated. No obvious irreversible (after) effect was observed for EcoRI, while a considerable irreversible inactivation was found for BamHI. Thus the EcoRI reactions against lambda DNA, pBR322 and pBluescript were studied under high pressure and little effect was observed on the overall reactions. The DNA concentration dependence of the kinetic data apparently fits the Michaelis-Menten type equation and the evaluated rate parameters were: Vmax = 6.2 +/- 0.24 and 7.0 +/- 0.22 (x 10(-2) nM/min) at 0.1 and 200 MPa, respectively; Km = 19 +/- 1.8 and 28 +/- 1.7 nM at 0.1 and 200 MPa, respectively. The apparent activation volume corresponding to kcat/Km was ca +1 mL/mol. A characteristic effect of pressure on the sequence specificity of these enzymes was seen in their star activity. Relaxed specificity was tightened by increasing pressure (200 MPa) with respect to that induced by low salt concentration or by the presence of organic solvent.

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“…In the fast motional region,7,8 for each allowed transition , the following line-width expression was used: Wx = (2/31/2)[7ß|'1( 2'1) = WrelM,x + Weich,x (1) where W^i^x gives the contribution to relaxation broadening by anisotropic dipolar modulation through the well-known relationship7,8…”

Section: Supplementary Materials Available: Table I Containing Absorb...mentioning

confidence: 99%

Pressure enhancement of charge-transfer complexing of 1-methyl-3-(carbomethoxy)pyridinium cation and 8-chlorotheophyllinate anion in aqueous solution

Williams¹

1981

J. Phys. Chem.

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Values have been obtained for the association constant of the acceptor l-methyl-3-(carbomethoxy)pyridinium cation with the donor 8-chlorotheophyllinate anion in aqueous solution at pH 7.0, I = 0.5, T = 25 OC, at pressures from 0.1 to 209.5 MPa. From these data the apparent volume change on association is estimated to be A V = -4.0 f 0.5 cm3 mol-', and the increment in compressibility is AK = 0.0 Pa-'. No significant change in the increment in the extinction coefficient, A€, was observed. The results are interpreted in terms of the volume changes to be expected on association due to ion pairing, charge transfer, and the approach of aromatic rings in water. IntroductionStudies on the effect of pressure on the activity of enzymes' and of the denaturation of proteins2 depend for their interpretation on a knowledge of the volume changes

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The effect of pressure on the activity of ribonuclease

Cited by 15 publications

References 30 publications

Partially folded states of the capsid protein of cowpea severe mosaic virus in the disassembly pathway

Partially folded states of the capsid protein of cowpea severe mosaic virus in the disassembly pathway

Effect of high of pressure of EcoRI reactions

Pressure enhancement of charge-transfer complexing of 1-methyl-3-(carbomethoxy)pyridinium cation and 8-chlorotheophyllinate anion in aqueous solution

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