근원섬유구성단백질의 SDS-polyacrylamide gel 전기 영동상으로 부터 돼지근육의 red muscle과 while muscle의 근원섬유단백질사이에는 30K성분함량의 특징적 차이가 나타났으며, 생물활성에서도 red muscle쪽이 white muscle쪽보다 높은 ATPase 활성을 나타내었다. 근원섬유단핵질의 열안정성은 D값에서 확실한 차이를 보여 white muscle쪽이 red muscle쪽보다 높은 열안정성을 나타냈고, 열역학량에서도 근섬유 type간의 차이를 보였다. 한편 근원섬유단백질의 열안정성은 생체조직에 가까운 형태일수륵 안정하다는 사실도 확인되었다.
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.
