Go toArchive
Browse byFacets
Bookbag ( 0 )
'Calmodulin' in keywords
Results  2 Items
Sorted by   
Section
Publication Year
1994 (1)
1992 (1)
1Author    Y. Utaka Takeuchi, PaulJ. Birckbichler, M. Anford, K. P. Atterson, N. L. Kyung, H. Ee, En, A. C. ArterRequires cookie*
 Title    Calmodulin Regulates Nucleotide Hydrolysis Activity of Tissue Transglutaminase  
 Abstract    The interaction of calmodulin with purified guinea pig liver transglutaminase was studied. The nucleotide (ATP and GTP) hydrolysis activity of this tissue transglutaminase was tran­ siently increased and then gradually decreased depending on calmodulin concentration. The peak activation was obtained in the presence of a stoichiometric amount of calmodulin. The effect of calmodulin on the classical transglutaminase activity was minimal. Fluorescence spectroscopy dem onstrated that the enzyme produced a significant blue shift in the emission peak of dansylated calmodulin. Interestingly, Ca2+ was not required for the interaction be­ tween the two proteins. The results described here give an additional regulatory role to calmodulin. 
  Reference    Z. Naturforsch. 49c, 453—457 (1994); received March 17/May 16 1994 
  Published    1994 
  Keywords    Calmodulin, Transglutaminase, Nucleotide Hydrolysis 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/49/ZNC-1994-49c-0453.pdf 
 Identifier    ZNC-1994-49c-0453 
 Volume    49 
2Author    ErwinW. BeckerRequires cookie*
 Title    Dynamics and Kinetics of Enzymes Kinetic Equilibrium of Forces in Biochemistry  
 Abstract    To explain the high specificity, high reaction rate, and high thermodynamic efficiency in enzymatic processes, cooperation of the enzyme with a molecular transfer unit is assumed. A "kinetic equilibrium of forces" is suggested, which enables high reaction rates to occur under equilibrium conditions and a thorough examination of the substrate to be made without con­ sumption of free energy. In case o f ATPases, ion-binding proteins are the most probable trans­ fer units. By analyzing the elementary effect in muscle contraction it is shown that the new theorem may be of substantial value in elucidating biochemical processes. 
  Reference    Z. Naturforsch. 47c, 628—633 (1992); received May 18 1992 
  Published    1992 
  Keywords    Enzyme, Mechanism, Free Energy Transfer, ATPase, Calmodulin, Muscle Contraction 
  Similar Items    Find
 DEBUG INFO      
 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0628.pdf 
 Identifier    ZNC-1992-47c-0628 
 Volume    47