Kinetic properties and the functional role of particulate MM-isoenzyme of creatine phosphokinase bound to heart muscle myofibrils.

نویسندگان

  • V A Saks
  • G B Chernousova
  • R Vetter
  • V N Smirnov
  • E I Chazov
چکیده

Fractional extractions of heart muscle have revealed that about 30% of cellular creatine phosphokinase activity are located in mitochondria and about 20% are bound to myofibrils [ 1,2] . The presence of significant creatine phosphokinase activity in heart and skeletal muscle myofibrils has been demonstrated also in studies of isolated myofibrillar preparations [ 1,3,4] . This particulate enzyme has been found to be electrophoretically identical to MM-isoenzyme of CPK* [l-4] . However, no detailed information concerning its properties including kinetic parameters is available. Comprehensive kinetic analyses have been made only for soluble isoenzymes from skeletal muscle [5-71, brain [.5,8] as well as for the mitochondrial isoenzyme from heart [9,10]. It has been shown recently that creatine phosphokinase isoenzymes may play an active role in intracellular energy transport [2,9,10] . In this situation any information of functional properties of myofibrillar CPK becomes to be of special importance. The purpose of this study was to determine the kinetic parameters of myofibrillar CPK from heart muscle and to compare them with the kinetic parameters of the myofibrillar ATPase reaction and mitochondrial CPK.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Localization of creatine kinase isoenzymes in myofibrils. II. Chicken heart muscle

Chicken heart muscle contains almost exclusively the BB isoenzyme of creatine kinase (CK), its myofibrils, moreover, lack an M-line. This tissue thus provides an interesting contrast to skeletal muscle, in which some of the MM-CK present as predominant CK isoenzyme is bound at the myofibrillar M-line. Approx. 2% of the total CK activity in a chicken heart homogenate remains bound to the myofibr...

متن کامل

Release of enzymes from adult rat heart myocytes.

The release of lactic dehydrogenase, creatine phosphokinase, and aspartate aminotransferase from initially viable, metabolically competent adult rat heart myocytes has been examined. Freshly isolated cells contain levels of total lactic dehydrogenase, creatine phosphokinase, and aspartate aminotransferase, as well as lactic dehydrogenase and creatine phosphokinase isoenzyme profiles that are qu...

متن کامل

Intracellular targeting of isoproteins in muscle cytoarchitecture

Part of the muscle creatine kinase (MM-CK) in skeletal muscle of chicken is localized in the M-band of myofibrils, while chicken heart cells containing myofibrils and BB-CK, but not expressing MM-CK, do not show this association. The specificity of the MM-CK interaction was tested using cultured chicken heart cells as "living test tubes" by microinjection of in vitro generated MM-CK and hybrid ...

متن کامل

Kinetic properties of the isoenzymes of human creatine phosphokinase.

Studies of the three human creatine phosphokinase (EC 2.7.3.2) isoenzymes, MM, MB, and BB, show that important differences exist in substrate dependency of the reaction rates. A method was developed to study these properties in which the ATP formed in the reverse reaction was measured by means of firefly luciferase. With substrate conditions at which the isoenzymes showed substantial difference...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • FEBS letters

دوره 62 3  شماره 

صفحات  -

تاریخ انتشار 1976