Measurement of tensile strength of muscle fibers and its change during postmortem aging of chicken breast muscle

1972 ◽  
Vol 20 (4) ◽  
pp. 809-812 ◽  
Author(s):  
Ryo Nakamura
Keyword(s):  
Tensile Strength ◽  
Muscle Fibers ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Postmortem Aging

EFFECT OF POSTMORTEM AGING ON CHICKEN BREAST MUSCLE SARCOPLASMIC RETICULUM

1973 ◽  
Vol 38 (4) ◽  
pp. 700-704 ◽  
Author(s):  
J. D. HAY ◽  
R. W. CURRIE ◽  
F. H. WOLFE ◽  
E. J. SANDERS
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Postmortem Aging

Acidic and basic troponin T isoforms in mature fast-twitch skeletal muscle and effect on contractility

1999 ◽  
Vol 276 (5) ◽  
pp. C1162-C1170 ◽  
Author(s):  
Ozgur Ogut ◽  
Henk Granzier ◽  
Jian-Ping Jin
Keyword(s):  
Troponin I ◽  
Striated Muscle ◽  
Troponin T ◽  
Muscle Fibers ◽  
Variable Region ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Adult Chicken ◽  
Isoform Expression ◽  
Fast Twitch

Developmentally regulated alternative RNA splicing generates distinct classes of acidic and basic troponin T (TnT) isoforms. In fast-twitch skeletal muscles, an acidic-to-basic TnT isoform switch ensures basic isoform expression in the adult. As an exception, an acidic segment in the NH2-terminal variable region of adult chicken breast muscle TnT isoforms is responsible for the unique exclusive expression of acidic TnTs in this muscle (O. Ogut and J.-P. Jin. J. Biol. Chem. 273: 27858–27866, 1998). To understand the relationship between acidic vs. basic TnT isoform expression and muscle contraction, the contractile properties of fibers from adult chicken breast muscle were compared with those of the levator coccygeus muscle, which expresses solely basic TnT isoforms. With use of Triton X-100-skinned muscle fibers, the force and stiffness responses to Ca2+ were measured. Relative to the levator coccygeus muscle, the breast muscle fibers showed significantly increased sensitivity to Ca2+ of force and stiffness with a shift of ∼0.15 in the pCa at which force or stiffness was 50% of maximal. The expression of tropomyosin, troponin I, and troponin C isoforms was also determined to delineate their contribution to thin-filament regulation. The data indicate that TnT isoforms differing in their NH2-terminal charge are able to alter the sensitivity of the myofibrillar contractile apparatus to Ca2+. These results provide evidence linking the regulated expression of distinct acidic and basic TnT isoform classes to the contractility of striated muscle.

EFFECTS OF POSTMORTEM AGING ON CHICKEN BREAST MUSCLE SARCOPLASMIC RETICULUM LIPIDS

1978 ◽  
Vol 58 (2) ◽  
pp. 143-149
Author(s):  
R. W. CURRIE ◽  
J. D. HAY ◽  
F. H. WOLFE ◽  
E. J. SANDERS
Keyword(s):  
Fatty Acid Composition ◽  
Sarcoplasmic Reticulum ◽  
Membrane Lipids ◽  
Neutral Lipids ◽  
Polar Lipids ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Phospholipase Activity ◽  
Postmortem Aging ◽  
Aging Phenomena

Polar lipids of chicken breast muscle sarcoplasmic reticulum have been extracted and quantitated from preparations at various times of postmortem aging. Neutral lipids and fatty acid composition of selected polar lipids were determined in at-death preparations. While phospholipase activity against endogenous membrane lipids was not demonstrated, exogenous phosphatidyl choline was hydrolyzed when incubated with the fragmented sarcoplasmic reticulum. Electron micrographs of negatively stained sarcoplasmic reticulum, showing different vesicle types and selective uptake of calcium oxalate, are also presented. The significance of the results is discussed in light of postmortem aging phenomena.

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.

Chicken Breast Muscle Connectin: Passive Tension and I-Band Region Primary Structure

2007 ◽  
Vol 370 (2) ◽  
pp. 213-219 ◽  
Author(s):  
Hiroshi Noguchi ◽  
Shigeru Takemori ◽  
Junpei Kajiwara ◽  
Masako Kimura ◽  
Koscak Maruyama ◽  
...  
Keyword(s):  
Primary Structure ◽  
Breast Muscle ◽  
Chicken Breast ◽  
Passive Tension ◽  
Band Region
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