Behavior of actin under high pressure

Ikeuchi, Yoshihide; Suzuki, A.; Oota, Takayoshi; Hagiwara, K.; Balny, Claude

doi:10.1016/s0921-0423(02)80085-5

Cited by 2 publications

(2 citation statements)

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“…The intensity began to decrease as soon as the pressure reached 250 MPa (data not shown). When the time dependence of change in the intensity of εADP–F‐actin at several pressure values above 250 MPa was investigated, the decrease in intensity obeyed first‐order kinetics as in the case of G‐actin [23]. The volume change for the denaturation of εADP–F‐actin was −67 mL·mol −1 , which was close to that of G‐actin (see Fig.…”

Section: Resultsmentioning

confidence: 80%

“…Apart from the fluorescence experiments, we attempted spectroscopic measurement such as NMR and also biochemical assays of actin after pressure release. Although details of the data are discussed elsewhere [23], the disappearance of a characteristic 1 H NMR signal at 2.06 p.p.m., which is considered to originate from the methyl proton of methionine in the vicinity of the DNaseI binding site in actin [28], and the loss in biochemical activity (DNase I inhibition capacity) were almost identical. The DNaseI binding site is located on the surface of the actin molecule [1].…”

Section: Resultsmentioning

confidence: 99%

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Fluorescence study of the high pressure‐induced denaturation of skeletal muscle actin

Ikeuchi

Suzuki

Oota

et al. 2002

European Journal of Biochemistry

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] made a thorough study of the e ect of pressure on G-and F-actins. However, all of the measurements in their study were made after the release of pressure. In the present experiment in situ observations were attempted by using eATP to obtain further detailed kinetic and thermodynamic information about the behaviour of actin under pressure. The dissociation rate constants of nucleotides from actin molecules (the decay curve of the intensity of¯uorescence of eATP-G-actin or eADP±F-actin) followed ®rst-order kinetics. The volume changes for the denaturation of G-actin and F-actin were estimated to be )72 mLámol )1 and )67 mLámol )1 in the presence of ATP, respectively. Changes in the intensity of¯uorescence of F-actin whilst under pressure suggested that eADP±F-actin was initially depolymerized to eADP±G-actin; subsequently there was quick exchange of the eADP for free eATP, and then polymerization occurred again with the liberation of phosphate from eATP bound to G-actin in the presence of excess ATP. In the higher pressure range (> 250 MPa), the partial collapse of the three-dimensional structure of actin, which had been depolymerized under pressure, proceeded immediately after release of the nucleotide, so that it lost the ability to exchange bound ADP with external free ATP and so was denatured irreversibly. An experiment monitoring eATP¯uorescence also demonstrated that, in the absence of Mg 2+ -ATP, the dissociation of 1 actin-heavy meromyosin (HMM) complex into actin and HMM did not occur under high pressure.

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Section: Resultsmentioning

confidence: 80%

Section: Resultsmentioning

confidence: 99%

Fluorescence study of the high pressure‐induced denaturation of skeletal muscle actin

Ikeuchi

Suzuki

Oota

et al. 2002

European Journal of Biochemistry

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Effect of High Pressure on Physicochemical Properties of Meat

Buckow

Sikes

Tume

2013

Critical Reviews in Food Science and Nutrition

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The application of high pressure offers some interesting opportunities in the processing of muscle-based food products. It is well known that high-pressure processing can prolong the shelf life of meat products in addition to chilling but the pressure-labile nature of protein systems limits the commercial range of applications. High pressure can affect the texture and gel-forming properties of myofibrillar proteins and, hence, has been suggested as a physical and additive-free alternative to tenderize and soften or restructure meat and fish products. However, the rate and magnitude at which pressure and temperature effects take place in muscles are variable and depend on a number of circumstances and conditions that are still not precisely known. This review provides an overview of the current knowledge of the effects of high pressure on muscle tissue over a range of temperatures as it relates to meat texture, microstructure, color, enzymes, lipid oxidation, and pressure-induced gelation of myofibrillar proteins.

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Behavior of actin under high pressure

Cited by 2 publications

References 4 publications

Fluorescence study of the high pressure‐induced denaturation of skeletal muscle actin

Fluorescence study of the high pressure‐induced denaturation of skeletal muscle actin

Effect of High Pressure on Physicochemical Properties of Meat

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