Analysis of the ATPase mechanism of myosin subfragment 1 from insect fibrillar flight muscle in the presence and absence of actin, using phosphate-water oxygen exchange measurements

1987 ◽  
Vol 8 (6) ◽  
pp. 537-540 ◽  
Author(s):  
D. C. S. White ◽  
J. W. Ricigliano ◽  
Martin R. Webb
Keyword(s):  
Flight Muscle ◽  
Oxygen Exchange ◽  
Water Oxygen ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence

The ATPase kinetics of insect fibrillar flight muscle myosin subfragment-1

1986 ◽  
Vol 7 (2) ◽  
pp. 179-192 ◽  
Author(s):  
D. C. S. White ◽  
R. W. Zimmermann ◽  
D. R. Trentham
Keyword(s):  
Flight Muscle ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Muscle Myosin ◽  
Kinetics Of

scholarly journals Binding of myosin subfragment 1 to glycerinated insect flight muscle in the rigor state

1985 ◽  
Vol 47 (2) ◽  
pp. 151-169 ◽  
Author(s):  
R.S. Goody ◽  
M.C. Reedy ◽  
W. Hofmann ◽  
K.C. Holmes ◽  
M.K. Reedy
Keyword(s):  
Flight Muscle ◽  
Insect Flight ◽  
Insect Flight Muscle ◽  
Rigor State ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Thiol-Specific Cross-Linkers of Variable Length Reveal a Similar Separation of SH1 and SH2 in Myosin Subfragment 1 in the Presence and Absence of MgADP†

Biochemistry ◽  
1999 ◽  
Vol 38 (32) ◽  
pp. 10307-10317 ◽  
Author(s):  
Werner Kliche ◽  
Jens Pfannstiel ◽  
Markus Tiepold ◽  
Stanka Stoeva ◽  
Heinz Faulstich
Keyword(s):  
Variable Length ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence

18O-Exchange by Hydrolyzing Enzymes: Extension of the Model to Pi Molecules with Inequivalent Oxygen Atoms in the Bound State

1981 ◽  
Vol 36 (7-8) ◽  
pp. 539-544 ◽  
Author(s):  
Paul Rösch
Keyword(s):  
Statistical Model ◽  
Data Fitting ◽  
Order Rate Constant ◽  
Bound State ◽  
Oxygen Exchange ◽  
Surrounding Water ◽  
Fitting Procedure ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Hydrolyzing Enzymes

Abstract Enzymes causing an exchange of oxygens from P\ with the surrounding water oxygens are very common. A statistical model for the data evaluation for an observation of this oxygen exchange by isotope methods is presented. It is shown how different cases of inequivalence of the four Pi oxygens may be uncovered. The number of reversals of the oxygen exchange step on the enzyme and the apparent second order rate constant for the binding of Pi to the enzyme are obtained as a result of the data fitting procedure. Cobalt phosphatase, zinc phosphatase, and myosin subfragment 1 are treated as examples.

Binding of gizzard smooth muscle myosin subfragment-1 to actin in the presence and absence of adenosine 5'-triphosphate

Biochemistry ◽  
1983 ◽  
Vol 22 (3) ◽  
pp. 530-535 ◽  
Author(s):  
Lois E. Greene ◽  
James R. Sellers ◽  
Evan Eisenberg ◽  
Robert S. Adelstein
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence ◽  
Muscle Myosin
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