ATP Dependent Deoxyribonuclease of Bacillus Subtilis; Subunit Structure and Substrate Specificity Of DNA Dependent -ATPase Activity

DNA Synthesis ◽  
1978 ◽  
pp. 423-429
Author(s):  
Janine Doly
Keyword(s):  
Bacillus Subtilis ◽  
Substrate Specificity ◽  
Atpase Activity ◽  
Subunit Structure ◽  
Dependent Atpase

scholarly journals A comparative study of myosin and its subunits in adult and neonatal-rat hearts and in rat heart cells from young and old cultures

1980 ◽  
Vol 191 (2) ◽  
pp. 627-635 ◽  
Author(s):  
H A Ghanbari ◽  
R L McCarl
Keyword(s):  
Atpase Activity ◽  
Light Chain ◽  
Rat Heart ◽  
Neonatal Rat ◽  
Temperature Sensitive ◽  
Heart Cells ◽  
Subunit Structure ◽  
Dependent Atpase ◽  
Rat Hearts ◽  
Rat Heart Cells

A possible explanation for the decrease in myosin Ca2+-dependent ATPase activity as rat heart cells age in culture is presented. The subunit structure and enzyme kinetics of myosin from adult and neonatal rat hearts and from rat heart cells of young and old cultures are compared. These studies indicate that the loss in Ca-ATPase activity of myosin from older cultures was an intrinsic property of the myosin itself. Myofibrillar fractions from the indicated four sources showed no qualitative or quantitative differences in electrophoretic patterns. Myosin from older cultures was more sensitive to alkaline denaturation than was myosin from younger cultures, as indicated by its more accelerated loss of K+(EDTA)-dependent ATPase activity after 10 min of incubation at pH 10. Furthermore, myosin from older cultures was more temperature-sensitive, as indicted by a more rapid loss of Ca-ATPase with decrease in assay temperature. It is suggested that there is either a change in conformation of myosin molecules at or near the active site of the enzyme or alternatively there is a change in light chain 1-light chain 2 and/or light-chain-heavy-chain interaction(s) in the myosin molecules under study.

Structural insights into the transient closed conformation and pH dependent ATPase activity of S.Typhi GyraseB N- terminal domain

2021 ◽  
Vol 701 ◽  
pp. 108786
Author(s):  
Deepali Gupta ◽  
Pragya Tiwari ◽  
Md Anzarul Haque ◽  
Ekta Sachdeva ◽  
Md Imtaiyaz Hassan ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Closed Conformation ◽  
Terminal Domain ◽  
Dependent Atpase ◽  
Ph Dependent ◽  
Structural Insights

scholarly journals No major thermogenic role for (Na+ + K+)-dependent adenosine triphosphatase apparent in hepatocytes from hyperthyroid rats

1982 ◽  
Vol 202 (3) ◽  
pp. 661-665 ◽  
Author(s):  
D G Clark ◽  
M Brinkman ◽  
O H Filsell ◽  
S J Lewis ◽  
M N Berry
Keyword(s):  
Oxygen Consumption ◽  
Oxygen Uptake ◽  
Atpase Activity ◽  
Heat Production ◽  
Adenosine Triphosphatase ◽  
Heat Output ◽  
Liver Parenchymal ◽  
Dependent Atpase ◽  
Parenchymal Cells ◽  
Isolated Liver

(Na+ + K+)-dependent ATPase activity, heat production and oxygen consumption were increased by 59%, 62% and 75% respectively in hepatocytes from tri-iodothyronine-treated rats. Ouabain at concentrations of 1 and 10 mM decreased oxygen uptake by 2-8% in hepatocytes from euthyroid rats and by 5-15% in hepatocytes from hyperthyroid animals. Heat output was decreased by 4-9% with the glycoside in isolated liver parenchymal cells from the control animals and by 11% in the cells from the tri-iodothyronine-treated animals. These results do not support the hypothesis that hepatic (Na+ + K+)-ATPase plays a major role in increased heat production in hepatocytes from hyperthyroid rats.

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