Results 271 to 280 of about 86,186 (304)

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 ...
P, CERLETTI, E, 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.
P, CERLETTI, L, ZICHELLA
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Adenylate kinase in human tissue II. Serum adenylate kinase and myocardial infarction

Journal of Molecular and Cellular Cardiology, 1973
Abstract Serum adenylate kinase was measured in 116 patients. An elevated level of serum adenylate kinase correlated well with myocardial infarctions and some other conditions associated with necrotising lesions. By taking advantage of the organ specificity of adenylate kinase, it was determined that a large portion of serum adenylate kinase activity
L H, Bernstein, J M, Horenstein, H D, Sybers, P J, Russell   +3 more
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Crystalline Adenylate Kinase from Carp Muscle

European Journal of Biochemistry, 1975
The concentration of adenylate kinase in carp muscle is about 0.3 mg/g. An improved isolation procedure makes use of a dilute solution of the substrates, ATP and AMP, to elute the enzyme from a phosphocellulose column in overall yields of 60% before crystallization. By the hexokinase–pH‐stat assay the specific activity is 3550 units/mg.
Noda, L., Schulz, G., von Zabern, I.
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Tissue Determined Variations of Adenylate Kinase

Nature, 1968
GENETICALLY determined isoenzymes of human erythrocyte adenylate kinase (AK), ATP : AMP phosphotransferase E.C. 2.7.4.3, have been reported1,2. We have characterized several forms of AK in different organs of Wistar rats, employing a mixed agarose-acrylamide gel electrophoresis3. The electrophoretic behaviour of AK was studied in tissues taken from the
J, Klethi, P, Mandel
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Recombinant Sea Urchin Flagellar Adenylate Kinase

Journal of Biochemistry, 2007
Adenylate kinase (AK) is localized in sea urchin sperm flagella and embryonic cilia. To investigate sea urchin Strongylocentrotus purpuratus AK (SpAK) enzymatic characteristics, the full-length recombinant protein of 130 kDa (SpAKr) and each of its three catalytic domains were expressed in Escherichia coli.
Masashi, Kinukawa, Victor D, Vacquier
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Low resolution structure of adenylate kinase

Journal of Molecular Biology, 1973
Abstract A low resolution model of adenylate kinase has been derived from a 6 A electron density map. The molecular shape can be described approximately as an oblate ellipsoid with dimensions 40 A × 40 A × 30 A. The molecule is composed of two globular units separated by a 10 A deep cleft.
Schulz, G., Biedermann, K., Kabsch, W., Schirmer, R.   +3 more
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8 Adenylate Kinase

1973
Publisher Summary This chapter describes adenylate kinase and discusses the studies analyzing this enzyme. Adenylate kinase from rabbit muscle was originally purified to a considerable extent by Colowick and Kalckar by taking advantage of its remarkable acid and heat stability.
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Three-dimensional structure of adenyl kinase

Nature, 1974
A combination of X-ray data at 3 A resolution and sequence results has yielded the atomic structure of adenyl kinase, a ubiquitous enzyme which catalyses the phosphorylation of AMP by ATP. The abundant secondary structures of the protein and the probable binding sites for ATP and AMP are described.
Schulz, G., Elzinga, M., Marx, F., Schirmer, R.   +3 more
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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, Wagner, E., Greppin, H., Bonzon, M.   +3 more
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