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 language | English |
|---|---|
| Pages (from-to) | 756-760 |
| Number of pages | 5 |
| Journal | Journal of Food Science |
| Volume | 68 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Jan 1 2003 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Food Science
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Structural changes in titin and nebulin filaments specific to calcium ions at 0.1 mM : Factors of meat tenderization during postmortem aging. / Tatsumi, Ryuichi; Takahashi, K.
In: Journal of Food Science, Vol. 68, No. 3, 01.01.2003, p. 756-760.Research output: Contribution to journal › Article
}
TY - JOUR
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
Y1 - 2003/1/1
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.
UR - http://www.scopus.com/inward/record.url?scp=0037391098&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037391098&partnerID=8YFLogxK
U2 - 10.1111/j.1365-2621.2003.tb08237.x
DO - 10.1111/j.1365-2621.2003.tb08237.x
M3 - Article
AN - SCOPUS:0037391098
VL - 68
SP - 756
EP - 760
JO - Journal of Food Science
JF - Journal of Food Science
SN - 0022-1147
IS - 3
ER -