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Cytoplasmic creatine kinases from giant pandas
Author(s) -
Wang XiCheng,
Ye JuQun,
Wang HongRui,
Zhou HaiMeng
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700205111
Subject(s) - creatine kinase , enzyme , cytoplasm , creatine , kinase , biochemistry , protein subunit , polyacrylamide gel electrophoresis , biology , homogeneous , microbiology and biotechnology , gel electrophoresis , chemistry , gene , physics , thermodynamics
The muscle and brain creatine kinases of giant panda have been isolated and purified. The purified muscle and brain enzymes (MM and BB) are homogeneous on both the polyacrylamide gel electrophoresis in the presence and absence of SDS. Both enzymes are dimers, consisting of two identical subunits each with a molecular weight of 42,000 daltons. The characteristics of muscle and brain enzymes have been studied, respectively. The hybridized enzyme, MB, was prepared by hybridization of MM and BB. The kinetic parameters of MM, BB and MB were determined, respectively. The results from modification of SH groups show that the SH groups of panda creatine kinases are essential for their activity and among the all SH groups in the enzyme only one per subunit is essential for enzymatic activity.