Abstract:Previously, it was clarified that myofibril gelation was enhanced by the basic protein glyceraldehyde 3-phosphate dehydrogenase (GPD). In this study, the mechanism of the gel-enhancing action of GPD to myosin B was evaluated through the study of the surface properties of GPD. GPD and myosin B were prepared from pork loin. Succinylated GPD (S-GPD) was successfully prepared without any loss of solubility at a weight ratio (succinic anhydrate to GPD) of 1.0. Though gelation of myosin B alone required a minimum pr… Show more
“…This conclusion is supported by our previous SDS-PAGE results, which indicated that G3PD bound to actin (Sakamoto et al, 2013). However, the release of myosin monomers from actomyosin was not confirmed.…”
Section: Verbeken Et Al (2005) Observed Fitc-labeled Carrageenan Didsupporting
confidence: 80%
“…However, G3PD was insoluble in the presence of G-actin, suggesting that the positively charged surface area of G3PD is necessary to increase the gel strength of myosin B (Sakamoto et al, 2013).…”
In this study, the effect of glyceraldehyde 3-phosphate dehydrogenase (G3PD) on the molecular state of porcine myofibrils was investigated by observing the structural changes in myosin and actin in myofibrils using phase-
“…This conclusion is supported by our previous SDS-PAGE results, which indicated that G3PD bound to actin (Sakamoto et al, 2013). However, the release of myosin monomers from actomyosin was not confirmed.…”
Section: Verbeken Et Al (2005) Observed Fitc-labeled Carrageenan Didsupporting
confidence: 80%
“…However, G3PD was insoluble in the presence of G-actin, suggesting that the positively charged surface area of G3PD is necessary to increase the gel strength of myosin B (Sakamoto et al, 2013).…”
In this study, the effect of glyceraldehyde 3-phosphate dehydrogenase (G3PD) on the molecular state of porcine myofibrils was investigated by observing the structural changes in myosin and actin in myofibrils using phase-
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