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A Convenient, Rapid, Sensitive, and Reliable Spectrophotometric Assay for Adenylate Kinase Activity. [PDF]

open access: yesMolecules, 2019
Song K   +8 more
europepmc   +1 more source

ADENYLATE KINASE IN PORCINE SKELETAL MUSCLE : PURIFICATION AND CHARACTERIZATION OF ADENYLATE KINASE a AND ADENYLATE KINASE ab

open access: yesADENYLATE KINASE IN PORCINE SKELETAL MUSCLE : PURIFICATION AND CHARACTERIZATION OF ADENYLATE KINASE a AND ADENYLATE KINASE ab
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Binding of Adenylate Kinase to RNA

Biochemical and Biophysical Research Communications, 1995
Adenylate kinase (ATP:AMP transphosphorylase) is a key enzyme in energy metabolism. The activity of its isoforms is subjected to multiple regulations. It is shown here that a specific fraction consisting of all adenylate kinase isoforms from tobacco leaves and tissue cultures does not bind to the anionic exchange-resin Mono Q.
Schlattner, Uwe   +3 more
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Domain Closure in Adenylate Kinase

Biochemistry, 1996
The method of time-resolved dynamic nonradiative excitation energy transfer (ET) was used to analyze the proposed domain closure in adenylate kinase (AK). A highly active mutant of Escherichia coli AK, (C77S, V169W, A55C)-AK, was prepared, in which the solvent- accessible residues valine 169 and alanine 55 were replaced by tryptophan (the donor of ...
Varda Ittah   +3 more
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Multiple Pathways and Time Scales for Conformational Transitions in apo-Adenylate Kinase.

Journal of Chemical Theory and Computation, 2018
The open/close transition in adenylate kinase (AK) is regarded as a representative example for large-scale conformational transition in proteins, yet its mechanism remains unclear despite numerous experimental and computational studies. Using extensive (∼
Yuqing Zheng, Q. Cui
semanticscholar   +1 more source

Adenylate kinase of mammalian erythrocytes

Biochimica et Biophysica Acta, 1960
Abstract The various blood constituents have been shown to be devoid of adenylate kinase activity, with the exception of the erythrocytes, where the enzyme activity is not bound to the stromal fraction. The optimal H+ concentration is at pH 7.5. Strong Mg++ activation and rapid denaturation by heat were found, whle no apprecible inhibitatation by ...
Paolo Cerletti, Enrico Bucci
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Adenylate kinase of human placenta

Clinica Chimica Acta, 1960
Abstract Human placenta has been shown to possess adenylate kinase activity. The optimal pH is about 7.7. When the homogenate is fractionated by differential centrifugation, the activity is mainly found m the supernate at 110,000 × g . The enzyme is not affected by azide and is inhibited by citrate.
Lucio Zichella, Paolo Cerletti
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