• Korean Journal of Food Science and Technology
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• v.21 no.4
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• pp.505-510
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• 1989

Red muscle and white muscle were separated from bovine, porcine and poultry skeletal muscles, respectively. Intramuscular lipids were extracted and fractionated to neutral-, glyco- and phospho-lipid by silica gel chromagraphy and then fatty acid composition were analyzed with gas chromatography. The results obtained were as follows; Total lipid content of red muscle was higher than that of white muscle in case of beef and chicken. In pork, however, total lipid content of white muscle was higher than red muscle The content ratio of neutral lipid to phospholipid revealed a number of distinctions between red and white muscle among animals. There were noteworthy differences in respect of polyunsaturated fatty acid. The intramuscular fat of pork had the higher content of highly polyunsaturated fatty acid such as arachidonic acid in contrast to beef.

• Korean Journal of Food Science and Technology
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• v.23 no.1
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• pp.6-14
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• 1991

Intramuscular lipid of longissimus dorsi muscle(white muscle), soleus muscle(red muscle) and cardiac muscle were autooxidized at $37^{\circ}C$ for 20 days, and the rancidity development and the effect of various factors on rancidity development were compared. Although the myoglobin content of red muscle was about 5 times as high as that of white muscle, the degree of autooxidation occurred in intramuscular lipid did not differ between red muscle and white muscle, when they had the same lipid content. Accordingly, it was suggested that the susceptibility of muscle tissues to lipid oxidation depends mainly on the lipid content of muscle tissue, regardless of muscle types. Lipid oxidation was not a major quality deterioration for dried-pork product, when it contained adequate amount of sodium nitrite and was air-tight vacuum-packed.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.181-186
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• 1986

Myosin were prepared from red muscle and white muscle, and their ATPase activities were compared. Ca-ATPase activity of bovine myosin from red muscle was higher than that of myosin from white muscle, while Ca-ATPase activity of chicken myosin from red muscle differed hardly from that of myosin from whitemuscle. Atso EDTA-ATPase activity of bovine red muscle myosin was higher than that of white muscle myosin ,although EDTA-ATPase activity of chicken myosin from red muscle differed hardly from that of white muscle myosin. When myosins were treated with trypsin, bovine myosin from white muscle was hydrolysed moreeasily than red muscle myosin was. Chicken myosin from red muscle , however, was hydrolysed by trypsin more easily than white muscle myosin was.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.173-180
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• 1986

To investigate on the biochemical characteristics of muscle fiber, myofibrils and actomyosins were prepared front red muscle and white muscle, and their ATPase activities and SDS-polyacrylamide gel electrophoretic patterns were compared. Also biochemical characteristics of bovine muscle were compared with those of chicken muscle for the detection of species characteristics. SDS-polyacrylamide gel electrophoretic analysis indicated that red muscle contained nlore 30K component of myofibril than white muscle. Differences in KCI concen-tration dependency of actomyosin ATPase activities and ATPase activity-pH cone were observed, when bovine muscle were compared with chicken muscle.

• Journal of Animal Science and Technology
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• v.45 no.5
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• pp.731-738
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• 2003

The technique known as proteomics is useful for characterizing the protein expression pattern of a particular tissue or cell type as well as quantitatively identifying differences in the levels of individual proteins. In present study, we carried out the comparative expression patterns of white and red muscles. We used the two-dimensional electrophoresis(2-DE) for analyzing the protein expression. Proteins isolated from porcine white and red muscles were separated by 12% poly-acrylamide gel and then were detected by coomassie blue and silver staining. More than 600 protein spots were detected on each 2-DE gel. By visual analysis of the stained gel, five proteins were identified to be differentially expressed in the white vs red muscle. By database searching based on the molecular weights and pI(isoelectric point) of the five proteins, three of them were found to be most close to troponin I, T and myoglobin. However, further researche is needed for identification and functional analysis of the unidentified proteins. In conclusion, we found five proteins, which are differentially expressed in the white vs red muscle. The functional analysis of the differentially expressed proteins will provide valuable information on biochemical characteristics of the muscle type.

• Korean Journal of Food Science and Technology
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• v.18 no.6
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• pp.443-449
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• 1986

In order to investigate the general characteristics of ATPase and ATPase thermostability between porcine white muscle and red muscle, myofibrillar proteins were prepared and compared their physicochemical characteristics. SDS-polyacrylamide gel electrophoretic analyses showed that a protein band of 30,000 daltons was detected noticeably in myofibril from red muscle, but negligibly in myofibril from white muscle. The noticeable differences were found between porcine white muscle and red muscle for the activities of EDTA-ATPase, Ca-ATPase and Mg-ATPase. Myofibrillar proteins from white muscle showed higher thermostability than those from red muscle. Thermodynamic parameters, enthalpy $({\Delta}H^#)$, entropy $({\Delta}S^#)$, etc., showed characteristic variations between porcine white muscle and red muscle.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.226-233
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• 1986

Myofibrillar proteins were prepared from red muscle and white muscle, and their thermostabilities were compared. Rate constants of inactivation of myofibrillar proteins were increased as the ionic strength of reaction mixture increased and also dielectric constant of reaction mixture decreased. Thermodynamic data forinactivation of myofibrillar proteins, such as $D-value,\;{\Delta}H^{\ddag},\;{\Delta}G{\ddag}\;and\;{\Delta}S^{\ddag$, revealed that thermostabilities of myofibrillar proteins from white muscle were higher than those from red muscle, and that myofibrillar proteins from chicken muscle were more heatlabile than from bovine muscle.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.4
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• pp.574-578
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• 2001

Myofibrillar proteins were prepared from red muscle and white muscle of fresh water fish and sea water fish, and their thermostabilities and effect of temperature on the myofibrillar ATPase activities were compared. Differences in temperature dependency of myofibrillar ATPase activities were found between two species. Thermodynamic data for inactivation of myofibrillar proteins, such as D value, Z value, $\Delta$ $H^{{\neq}}$, $\Delta$ $G^{{\neq}}$ and $\Delta$ $S^{\neq}$ revealed that thermostabilities of myofibrillar proteins from fresh water fish were higher than those from sea water fish, and that myofibrillar proteins from red muscle were more heat labile than those from white muscle.

• The Journal of Korean Physical Therapy
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• v.6 no.1
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• pp.61-74
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• 1994

This study was carried out to determine effects of electrical stimulation on the soleus, target muscle of the sciatic newt, of white rat normal muscles. The biometric, histochemical, ultrastructural observations were made. The following results were obtained. A daily electrical stimulation of the skeletal muscle of the normally-functioning rat caused an increase of girth and weight of the muscle fibers for 2 weeks. No noticeable change was observed afterwards. More specifically, the density of volume of the red muscle fiber increased. whereas the density of the white muscle fiber decreased. The electrical stimulation group(experimental group) showed hypertrophy of the muscle fibers and narrowing of the space between perimysium and endomysium. Normally, glycogen granules are accumulated regardless of classification of muscle fibers. In addition, the NADH-TR reaction results were in agreement with the biometric findings, in that the red muscle fibers significantly increased. The ultrastructural observations revealed that mitochondria was formed in the red muscle fiber parallel to the muscle fibers of normal muscle, while mitochondria was observed in the sarcomere region of the white muscle fiber. However, activation of mitochondria took place in the sarcolemma region of the muscle fiber, and generation of mitochondria was observed in the sarcomere region of the white muscle fiber.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.45 no.4
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• pp.307-316
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• 2012

This study evaluated the possible use of white muscle from cooked skipjack tuna as a constituent of diet foods. White muscles from the belly and dorsal area of cooked skipjack tuna were identified as anterior, median, and posterior. The skipjack tuna white muscle contained more moisture and ash (except for part I in both the belly and dorsal muscles) than chicken muscle, while it had less crude protein and crude lipid (except for part II in belly muscle). The yield was the highest in part I of both the dorsal and belly parts among the various parts of white muscles. The skipjack tuna white muscle contained 14-18% fewer calories than chicken breast muscle. Part I from both the belly and dorsal muscles had higher total amino acid contents than the other parts, but lower contents than chicken breast muscle. White muscle of skipjack tuna was rich in minerals, such as phosphorus, iron, and zinc. The total free amino acid content of part I in the belly and dorsal muscles was 1,152.1 and 1,215.7 mg/100 g, respectively, and was 1.7-1.8 times higher than in chicken breast muscle. The major amino acids in the white muscles from skipjack tuna were taurine, histidine, anserine, and carnosine. Based on these results, if it is possible to mask the fish odor, all parts of the white muscle from skipjack tuna could be used as constituents of diet foods.