Structural changes in titin and nebulin filaments specific to calcium ions at 0.1 mM: Factors of meat tenderization during postmortem aging

Ryuichi Tatsumi, K. Takahashi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Postmortem structural changes in titin and nebulin filaments were investigated by incubating isolated myofibrils in a solution containing 0.1 mM calcium ions and various concentrations of a protease inhibitor. The inhibition curves showed 2 abnormal steps with increases in the concentration of leupeptin or calpastatin domain I. While the amounts of unchanged titin and nebulin were constant in the 1st step, the 2nd occurred at higher protease inhibitor concentrations. These facts indicated that excess amounts of leupeptin and calpastatin domain I caused deterioration in titin and nebulin properties, thus interfering with the binding of calcium ions. We concluded that the severance of titin and nebulin filaments in the 1st step were induced by calcium ions at 0.1 mM.

Original languageEnglish
Pages (from-to)756-760
Number of pages5
JournalJournal of Food Science
Volume68
Issue number3
DOIs
Publication statusPublished - Jan 1 2003
Externally publishedYes

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Connectin
meat aging
tenderizing
Meat
calpastatin
meat
Ions
ions
proteinase inhibitors
Calcium
calcium
Protease Inhibitors
myofibrils
Postmortem Changes
Myofibrils
deterioration
nebulin
leupeptin

All Science Journal Classification (ASJC) codes

  • Food Science

Cite this

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abstract = "Postmortem structural changes in titin and nebulin filaments were investigated by incubating isolated myofibrils in a solution containing 0.1 mM calcium ions and various concentrations of a protease inhibitor. The inhibition curves showed 2 abnormal steps with increases in the concentration of leupeptin or calpastatin domain I. While the amounts of unchanged titin and nebulin were constant in the 1st step, the 2nd occurred at higher protease inhibitor concentrations. These facts indicated that excess amounts of leupeptin and calpastatin domain I caused deterioration in titin and nebulin properties, thus interfering with the binding of calcium ions. We concluded that the severance of titin and nebulin filaments in the 1st step were induced by calcium ions at 0.1 mM.",
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T1 - Structural changes in titin and nebulin filaments specific to calcium ions at 0.1 mM

T2 - Factors of meat tenderization during postmortem aging

AU - Tatsumi, Ryuichi

AU - Takahashi, K.

PY - 2003/1/1

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N2 - Postmortem structural changes in titin and nebulin filaments were investigated by incubating isolated myofibrils in a solution containing 0.1 mM calcium ions and various concentrations of a protease inhibitor. The inhibition curves showed 2 abnormal steps with increases in the concentration of leupeptin or calpastatin domain I. While the amounts of unchanged titin and nebulin were constant in the 1st step, the 2nd occurred at higher protease inhibitor concentrations. These facts indicated that excess amounts of leupeptin and calpastatin domain I caused deterioration in titin and nebulin properties, thus interfering with the binding of calcium ions. We concluded that the severance of titin and nebulin filaments in the 1st step were induced by calcium ions at 0.1 mM.

AB - Postmortem structural changes in titin and nebulin filaments were investigated by incubating isolated myofibrils in a solution containing 0.1 mM calcium ions and various concentrations of a protease inhibitor. The inhibition curves showed 2 abnormal steps with increases in the concentration of leupeptin or calpastatin domain I. While the amounts of unchanged titin and nebulin were constant in the 1st step, the 2nd occurred at higher protease inhibitor concentrations. These facts indicated that excess amounts of leupeptin and calpastatin domain I caused deterioration in titin and nebulin properties, thus interfering with the binding of calcium ions. We concluded that the severance of titin and nebulin filaments in the 1st step were induced by calcium ions at 0.1 mM.

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