Change of acto-heavy meromyosin ATPase of rabbit skeletal muscle during postmortem storage

Ito, Tetsuhide; Sung, Sam Kyung; Fukazawa, Toshiyuki

doi:10.1021/jf60216a024

Cited by 16 publications

(14 citation statements)

References 20 publications

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“…When rabbit muscle is stored at low temperatures the actin-myosin interaction is promoted during the development of rigor mortis and it continues to increase as measured by an increase of myofibrillar ATPase activity . 35 At 12 days the activity decreased to about 0-3pmol min-' mg-l in both IS and PFS. At 16 and 20 days there was no ATPase activity in IS shrimp whereas in PFS the activity decreased rapidly to 0.02 pmol min-l mg-l by 16 days; thereafter no activity was found.…”

Section: Changes In Atpase Activity and Sarcoplasmic And Myofibrillarmentioning

confidence: 91%

Shelf life of shrimp (Penaeus merguiensis) stored in ice (0°C) and partially frozen (—3°C)

1988

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Sensory, biochemical and microbiological changes and changes in SDS-PAGE patterns of myofibrillar and sarcoplasmic proteins were studied in shrimp (Penaeus merguiensis) muscle during storage at partial freezing temperature (-3°C; PFS) and in ice (0°C; IS). During PFS up to 20 days there were slight changes in biochemical parameters, apparently no changes in microbiological populations, and no changes in electrophoretic protein patterns. Rapid changes in these parameters occurred in IS over the same period. Sensory assessment of shrimps stored at PFS showed that a considerable increase in prime quality life was possible at this temperature over shrimps in IS. Prime quality life of shrimps in PFS was found to be 16 days, compared with 8 days in IS. Extension of prime quality life was attributed to the significantly slower rate of biochemical and microbiological changes at PFS compared with IS. Changes in sensory properties were associated with changes in some of the chemical properties.

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Section: Changes In Atpase Activity and Sarcoplasmic And Myofibrillarmentioning

confidence: 91%

Shelf life of shrimp (Penaeus merguiensis) stored in ice (0°C) and partially frozen (—3°C)

1988

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“…Park et alY) showed that calcium sensitivity of myosin B prepared from PSE muscle was partially lost. In a previous paper, we have reported that normal myofibril prepared from 24 contract upon addition of Mg2+ -ATP, while PSE myofibril contract in part or cannot contract, even though PSE myofibril retains partially its Mgl + -ATPase activity.12) This result suggests that contraction is apparently uncoupled with Mg2 + -ATPase in PSE muscle.…”

Section: Please Scroll Down For Articlementioning

confidence: 88%

“…1). 24) We have already shown that some denaturations might occur in myofibrillar proteins, particularly on myosin, of PSE porcine muscle. 12 ) The present results also indicate the partial inactivation of myosin in PSE muscle (Figs.…”

Section: Initial Burst Of Normal and Pse Myosinsmentioning

confidence: 93%

“…Myosin was prepared from porcine muscle immediately after death and the muscles stored for 24 HMM was obtained by the method of Lowey and Cohen!5) with slight modifications: trypsin digestion was done for 4 min at 25°C, and purification of HMM was made by ammonium sulfate fractionation between 42 ~ 58 % saturation, and then dialyzed against 40 mM KCI, IOmM Tris-maleate (pH 7.0), I mM dithiothreitol (DTT) prior to use in the assay. Actin was prepared according to the method of Spudich and Watt,!6) except that the time of polymerization was prolonged overnight instead of 2 hr in the original method.…”

Section: Methodsmentioning

confidence: 99%

“…DISCUSSION It has been presumed that the actin-myosin interaction in muscle is modified during postmortem storage. 30 ,31) Ito et al 24 ) have shown that the V max of acto-HMM ATPase is decreased during storage of rabbit muscle at DOC. In addition, the Kapp of the acto-HMM complex was decreased during storage, indicating that the affinity of actin for myosin increased during storage at DoC.…”

Section: Initial Burst Of Normal and Pse Myosinsmentioning

confidence: 99%

See 2 more Smart Citations

Myosin ATPase and Acto-Heavy Meromyosin ATPase in Normal and in Pale, Soft and Exudative (PSE) Porcine Muscle

Sung

Ito

Izumi

1981

Agricultural and Biological Chemistry

Self Cite

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Comparative effects of post‐mortem storage and low‐calcium‐requiring neutral proteinase on bovine and rabbit myofibrillar proteins

Ouali¹,

Obled²,

Cottin

et al. 1983

J Sci Food Agric

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The effects of post-mortem storage and of a low-calcium-requiring neutral proteinase on the myofibrils of beef Longissimus dorsi and Rectus abdominis muscles and rabbit Longissirnus dorsi muscle were studied by measuring the Mg-Ca-enhanced myofibrillar ATPase activity and the changes in banding patterns on electrophoresis in sodium dodecyl sulphate. During ageing, the changes in the ATPase activity and myofibrillar proteins were qualitatively different between rabbit and bovine muscles, whilst differences in intensity were only observed between the two bovine muscles. The most prevalent component appearing upon conditioning had a mol. wt of 27 000 in rabbit muscle and of 30 000 in bovine muscles. In both species, the incubation of myofibrils with the low-calcium-requiring neutral proteinase mimicked the post-mortem changes. This would suggest that this enzyme has a qualitatively different effect on rabbit and bovine myofibrils.

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Change of acto-heavy meromyosin ATPase of rabbit skeletal muscle during postmortem storage

Cited by 16 publications

References 20 publications

Shelf life of shrimp (Penaeus merguiensis) stored in ice (0°C) and partially frozen (—3°C)

Shelf life of shrimp (Penaeus merguiensis) stored in ice (0°C) and partially frozen (—3°C)

Myosin ATPase and Acto-Heavy Meromyosin ATPase in Normal and in Pale, Soft and Exudative (PSE) Porcine Muscle

Comparative effects of post‐mortem storage and low‐calcium‐requiring neutral proteinase on bovine and rabbit myofibrillar proteins

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