ON THE MECHANISM OF STIMULATION OF AMP‐AMINOHYDROLASE ACTIVITY BY HEXOKINASE IN BRAIN TISSUE

—A hexokinase has been isolated from brain tissue on Sephadex G‐100 and DEAE cellulose which is similar to yeast enzyme in stimulating the AMP‐aminohydrolase activity of rat brain soluble fractions. This effect of hexokinase is influenced neither by N‐acetyl‐glucosamine nor noradrenaline. An isoenzy...

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Veröffentlicht in:	Journal of neurochemistry 1974-08, Vol.23 (2), p.297-302
Hauptverfasser:	Haroutunian, A. V., Buniatian, H. Ch
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Monophosphate Aminohydrolases - metabolism Ammonia - metabolism Animals Brain - cytology Brain - drug effects Brain - enzymology Brain - physiology Cattle Chromatography, DEAE-Cellulose Chromatography, Gel Cytosol - enzymology Guinea Pigs Hexokinase - isolation & purification Hexokinase - physiology Kinetics Molecular Weight Rabbits Rats Saccharomyces cerevisiae - enzymology Species Specificity Spectrophotometry, Ultraviolet Swine Time Factors Urea - pharmacology
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Zusammenfassung:	—A hexokinase has been isolated from brain tissue on Sephadex G‐100 and DEAE cellulose which is similar to yeast enzyme in stimulating the AMP‐aminohydrolase activity of rat brain soluble fractions. This effect of hexokinase is influenced neither by N‐acetyl‐glucosamine nor noradrenaline. An isoenzyme of hexokinase isolated from brain tissue on DEAE cellulose, having properties similar to that of the muscle enzyme, has no effect on AMP‐aminohydrolase activity. The activating effect of yeast hexokinase is not due to its oligomeric structure. Enzyme subunits obtained by the treatment of native yeast enzyme by urea also activate AMP‐aminohydrolase of rat brain soluble fractions.
ISSN:	0022-3042 1471-4159
DOI:	10.1111/j.1471-4159.1974.tb04357.x