Mechanism of Emptying of Skeletal Muscle Cell Segments

Stanley, David; Hultin, Herbert O.

doi:10.1083/jcb.39.1.c1

Cited by 16 publications

(7 citation statements)

References 12 publications

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“…It is of interest that the order of addition of the solubilizing components was important. We had earlier shown that polyvalent cations, including magnesium ions, were capable of inhibiting the solubilization of chicken breast muscle myofibrillar proteins at low ionic strength (Stanley and Hultin 1968). In the experiments reported here, we also found that magnesium ions inhibited myosin solubilization unless the muscle was first exposed to the pyrophosphate and sodium chloride (in either order of addition).…”

Section: Myosin Solubility and Gelationsupporting

confidence: 74%

“…It is possible that magnesium ions are inhibitory to solubilization of actomyosin, and the actomyosin must first be dissociated into its component proteins before magnesium becomes an effective solubilizing agent at that salt concentration. In our earlier studies where magnesium was inhibitory to solubilization, the myosin would have been present in the form of actomyosin (Stanley and Hultin 1968;Comissiong and Hultin 1978).…”

Section: Myosin Solubility and Gelationmentioning

confidence: 90%

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EFFECT OF MgCl₂/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

Chang

Hultin

Dagher

2001

J Food Biochemistry

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Sodium chloride (0.29 M) at pH 7 solubilized about 24% of the myosin of washed, minced chicken breast muscle. At a similar pH, 0.2 M sodium chloride in the presence of 10 mM sodiumpyrophosphate and 10 mM magnesium chloride solubilized almost 60% of the myosin. In spite of the greater solubility of myosin under the latter conditions, when gels were prepared with these concentrations of salt at pH 7, the gels without the sodium pyrophosphate and magnesium chloride were slightly superior in both stress (39.3 kPa vs 28.3 kPa) and true strain (2.3 vs 2.0) values. Gels made at a lower pH (6.1–6.5) made much poorer gels. This was true whether the low pH was obtained naturally in the preparation of the sample or re‐adjusted after bringing the mince to a neutral pH. It appears that conditions of pH and salt content that cause solubilization of myosin at more dilute conditions does not contribute to gel quality, but the neutral pH is an important factor for obtaining good gels at ionic strengths <0.3.

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Section: Myosin Solubility and Gelationsupporting

confidence: 74%

Section: Myosin Solubility and Gelationmentioning

confidence: 90%

EFFECT OF MgCl₂/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

Chang

Hultin

Dagher

2001

J Food Biochemistry

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“…Studies conducted several years ago to prepare sarcolemma from chicken breast muscle suggested that the myofibrillar proteins were soluble in solutions of low ionic strength, although careful evaluation of protein solubility was not done. Treatment of cell segments of chicken breast muscle with calcium chloride (0.5-50 mM) followed by washes with buffered sodium chloride solutions (25 mM) caused the material inside the muscle cell segments to be removed on dilution in slightly alkaline solutions of low ionic strength (Westort and Hultin, 1966;Stanley and Hultin, 1968). The purpose of the experiments reported here was to evaluate the solubility of chicken breast muscle proteins in solutions of low ionic strength.…”

Section: Introductionmentioning

confidence: 99%

Solubility of Chicken Breast Muscle Proteins in Solutions of Low Ionic Strength

Krishnamurthy

Chang

Hultin

et al. 1996

J. Agric. Food Chem.

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Essentially all of the proteins of chicken breast muscle were soluble in sodium chloride solutions of physiological ionic strength or less and neutral pH. However, there was a critical order of treatment necessary to accomplish this. After removal of those proteins solubilized by homogenizing the tissue 1:10 (w/v) in water, it was necessary to solubilize a fraction of the remaining proteins in moderate concentrations (25-150 mM) of sodium chloride at neutral pH before the remaining proteins could be solubilized in water. Solubilization of chicken breast muscle proteins in water could be prevented or reversed by salt solutions of low concentration, suggesting that most of the solubility was not directly caused by proteolysis. SDS-polyacrylamide gel electrophoresis indicated that removal of specific peptides by moderate concentrations of sodium chloride at neutral pH was correlated with removal of the restriction on the water solubility of the remaining proteins.

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“…Moreover, the Ca 2+ and Mg 2+ contents correlated negatively with WHC. These cations reduce the hydrating capacity of proteins because they cause compacting of the structure, forming bridges between the peptide chains of a given component (actin, myosin) or else between chains of actin and myosin (Stanley & Hultin, 1968;Haurowitz, 1950). Equally, in the first component the factor analysis also showed a direct correlation between hardness and water loss, similar to what was observed in brined cod at the same pH prior to dry salting ).…”

Section: Discussionmentioning

confidence: 99%

Influence of mono- and divalent salts on water loss and properties of dry salted cod fillets

Martínez-Álvarez¹,

Gómez‐Guillén²

2013

LWT - Food Science and Technology

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Salted cod is a product highly appreciated by consumers, especially in Southern Europe and Latin America. In recent years there has been increasing consumer demand for products with low sodium content, and this has led the salting industry to seek new salt mixtures to help to reduce Na + levels without producing alterations in the properties of the final product. In this study, Atlantic cod (Gadus morhua) was initially brined with various mixtures of salts based on NaCl, at various pH levels and including KCl, MgCl 2 and/or CaCl 2. After subsequent dry salting with NaCl, the Na + , K + , Ca 2+ and Mg 2+ cation contents were evaluated, and also their effect on water loss, salt uptake, entry of chloride, water holding capacity (WHC), water extractable protein (WEP) and hardness of the end product. A greater presence of K + in muscle was associated with greater water loss, salt uptake and hardness of the dry salted product. Moreover, incorporation of Ca 2+ and Mg 2+ 2 negatively affected water holding capacity. These changes were not dependent on brine pH and might significantly alter the acceptability of the final product.

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Mechanism of Emptying of Skeletal Muscle Cell Segments

Cited by 16 publications

References 12 publications

EFFECT OF MgCl₂/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

EFFECT OF MgCl₂/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

Solubility of Chicken Breast Muscle Proteins in Solutions of Low Ionic Strength

Influence of mono- and divalent salts on water loss and properties of dry salted cod fillets

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Mechanism of Emptying of Skeletal Muscle Cell Segments

Cited by 16 publications

References 12 publications

EFFECT OF MgCl2/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

EFFECT OF MgCl2/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

Solubility of Chicken Breast Muscle Proteins in Solutions of Low Ionic Strength

Influence of mono- and divalent salts on water loss and properties of dry salted cod fillets

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Product

Resources

About

EFFECT OF MgCl₂/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION

EFFECT OF MgCl₂/SODIUM PYROPHOSPHATE ON CHICKEN BREAST MUSCLE MYOSIN SOLUBILIZATION AND GELATION