Effect of pH on the Rheological and Structural Properties of Gels of Water-Washed Chicken-Breast Muscle at Physiological Ionic Strength

2001 ◽  
Vol 49 (8) ◽  
pp. 3927-3935 ◽  
Author(s):  
Yuming Feng ◽  
Herbert O. Hultin
Keyword(s):  
Ionic Strength ◽  
Structural Properties ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Effect Of Ph

Role of Reduced Ionic Strength and Low pH in Gelation of Chicken Breast Muscle Protein

2005 ◽  
Vol 70 (1) ◽  
pp. E1-E6 ◽  
Author(s):  
S. Ke And ◽  
H. O. Hultin
Keyword(s):  
Ionic Strength ◽  
Muscle Protein ◽  
Low Ph ◽  
Breast Muscle ◽  
Chicken Breast

Role of pH and Ionic Strength on Water Relationships in Washed Minced Chicken-breast Muscle Gels

2003 ◽  
Vol 68 (3) ◽  
pp. 917-922 ◽  
Author(s):  
H.G. Kristinsson ◽  
H.O. Hultin
Keyword(s):  
Ionic Strength ◽  
Breast Muscle ◽  
Chicken Breast

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

1996 ◽  
Vol 44 (2) ◽  
pp. 408-415 ◽  
Author(s):  
Ganesan Krishnamurthy ◽  
Hsin-Sui Chang ◽  
Herbert O. Hultin ◽  
Yuming Feng ◽  
Subramanian Srinivasan ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Muscle Proteins ◽  
Low Ionic Strength

Estimation of water-extractable Ca in chicken breast muscle by atomic absorption

1973 ◽  
Vol 53 (2) ◽  
pp. 531-537 ◽  
Author(s):  
Ryo Nakamura
Keyword(s):  
Atomic Absorption ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Water Extractable

STARCH GEL ELECTROPHORESIS OF MYOGEN FROM CHICKEN BREAST MUSCLE IN CONSTANT AND GRADIENT BUFFER SYSTEMS

1963 ◽  
Vol 41 (1) ◽  
pp. 369-387 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Starch Gel Electrophoresis ◽  
Two Dimensional ◽  
Sodium Cacodylate ◽  
Gradient Systems ◽  
Optimal Separation ◽  
Starch Gel

By varying conditions of starch gel electrophoresis, factors contributing to the resolution of myogen proteins from chicken breast muscle have been studied. Variables examined included composition of the myogen extractant, protein concentration, ionic strength of electrophoretic media, pH of gel media, plane and direction of electrophoresis, and the nature of cations and anions in gel media and bridge solutions. The significance of anions was more closely studied with constant buffer systems, and gradient systems in which bridge electrolyte differed from, and gradually altered, the gel medium. Optimal separation was obtained in gradient systems with 0.10 M sodium chloride bridge solutions, and gel media of sodium cacodylate, pH 6.9, μ 0.010, which resolved 12 cationic zones, and sodium veronal, pH 7.4, μ 0.010, which resolved 10 anionic zones. These buffers in two-dimensional sequence revealed a total of about 24 components in this myogen.

Multiple Forms of Phosphoglyceromutase from Chicken Breast Muscle

1972 ◽  
Vol 50 (10) ◽  
pp. 1132-1142 ◽  
Author(s):  
Eric James ◽  
R. O. Hurst ◽  
T. G. Flynn
Keyword(s):  
Specific Activity ◽  
Gel Filtration ◽  
Diffusion Constant ◽  
Sedimentation Coefficient ◽  
Breast Muscle ◽  
Heat Inactivation ◽  
Chicken Breast ◽  
Multiple Forms ◽  
Active Components ◽  
Net Charges

Phosphoglyceromutase (2,3-diphospho-D-glycerate: 2-phospho-D-glycerate phosphotransferase, EC 2.7.5.3) has been purified from both frozen and fresh chicken breast muscle. During purification it was found that substrate, 3-phospho-D-glycerate stabilized the enzyme against heat inactivation to almost the same extent as did the cofactor 2,3-diphospho-D-glycerate.Phosphoglyceromutase prepared from frozen chicken breast muscle separated into three peaks of activity (I, II, and III) following chromatography on DEAE-Sephadex in 0.05 μ phosphate buffer, pH 8.0, using a 0.0–0.4 M NaCl gradient. Each peak of activity was shown by polyacrylamide disc gel electrophoresis at pH 9.3 to contain two enzymically active components (isoenzymes Ia Ib, IIa IIb, and IIIa IIIb). Isoenzymes in the same peak had the same specific activity. Phosphoglyceromutase prepared from fresh chicken breast muscle yielded only one peak of activity following chromatography on DEAE-Sephadex. This peak contained two enzymically active components corresponding to isoenzymes Ia and Ib. Additional peaks of activity were not produced when phosphoglyceromutase from fresh muscle was subjected to freezing and thawing.Isoenzyme Ia and mixtures of Ia and Ib, IIa and IIb, and IIIa and IIIb were homogeneous in the ultra-centrifuge sedimenting as single peaks. The sedimentation coefficient obtained for isoenzyme Ia and for Ia and Ib combined was 4.15 S, the diffusion constant 6.62 × 10−7 cm2/s, and the molecular weight calculated from both gel filtration and sedimentation data was of the order of 59 000. These results were confirmed by charge isomer studies which also showed that the isoenzymes of phosphoglyceromutase from frozen chicken breast muscle were proteins of the same size but different net charges.

Adsorption and surface precipitation of phosphate onto CaCO3–montmorillonite: effect of pH, ionic strength and competition with humic acid

Geoderma ◽  
2014 ◽  
Vol 232-234 ◽  
pp. 600-608 ◽  
Author(s):  
Ileana Perassi ◽  
Laura Borgnino
Keyword(s):  
Humic Acid ◽  
Ionic Strength ◽  
Effect Of Ph ◽  
Surface Precipitation

scholarly journals The effect of pH and ionic strength of dissolution media on in-vitro release of two model drugs of different solubilities from HPMC matrices

2013 ◽  
Vol 111 ◽  
pp. 384-391 ◽  
Author(s):  
Kofi Asare-Addo ◽  
Barbara R. Conway ◽  
Hassan Larhrib ◽  
Marina Levina ◽  
Ali R. Rajabi-Siahboomi ◽  
...  
Keyword(s):  
Ionic Strength ◽  
In Vitro Release ◽  
Effect Of Ph ◽  
Vitro Release

The effect of pH and ionic strength on starch–kaolinite interactions

2010 ◽  
Vol 94 (3-4) ◽  
pp. 111-114 ◽  
Author(s):  
X. Ma ◽  
W.J. Bruckard
Keyword(s):  
Ionic Strength ◽  
Effect Of Ph
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