• Title/Summary/Keyword: Thermostability variations

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Genetic Diversity and Thermostabilitical Variants of Corbicula japonica from the Two Main Rivers in Korea (한국의 두 강으로부터 재첩의 유전적 종다양성과 열안정성 변이체)

  • Heo, Man-Gyu;Mun, Du-Ho;Heo, Heung-Uk
    • Journal of Environmental Science International
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    • v.7 no.3
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    • pp.243-250
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    • 1998
  • We examined the genetic variation within the species, the patterns of genetic diversty between populations, thermostability variations of enzymes and temperature tolerances of Corbicula japonica from the two main rivers In Korea. Starch gel electrophoresis was used to examine the genetic variation of 22 locl. Henting experiments of electrophoresis under the condition of 40$\pm$5$^{\circ}$ for 15$\pm$5 min disclose thermostabllity differences, called heat-sensitive and heat-resistant types, within each 디ectrophoretic allozyme. Genetic diversity at the natural species level was high (77.3%), whereas the extent of heat-treat groups was relatively low (52.6%). The genetic diversity trends to decrease from the source of two main siderable high genetic diversity compared with a mean value of C. japonica species, It is recommended that several populations of the species in Korea should be preserved.

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Comparative Biochemical Study on the Myofibrillar Proteins from Porcine Muscle (Porcine Myofibrillar Protein에 대한 비교생화학적 연구)

  • Yang, Ryung;Park, Hyun-Joo;Kim, Young-Ho;Jhin, Hong-Seung;Shin, Wan-Chul
    • 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.

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