Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
 5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have analysed the pattern of expression of the hexokinase isoenzyme group in RIN-m5F insulinoma cells. Three hexokinase forms were resolved by DEAE-cellulose chromatography. The most abundant isoenzyme co-eluted with hexokinase type II from rat adipose tissue and displayed a Km for glucose of 0.15 mM, similar to the adipose-tissue enzyme. Hexokinase type II was in large part associated with a particulate subcellular fraction in RIN-m5F cells. The two other hexokinases separated by ion-exchange chromatography were an enzyme similar to hexokinase type I from brain and glucokinase (or hexokinase type IV). The latter isoenzyme was identified as the liver-type glucokinase by the following properties: co-elution with hepatic glucokinase from DEAE-cellulose and DEAE-Sephadex; sigmoid saturation kinetics with glucose with half-maximal velocity at 5.6 mM and Hill coefficient (h) of 1.54; suppression of enzyme activity by antibodies raised against rat liver glucokinase; apparent Mr of 56,500 and pI of 5.6, as shown by immunoblotting after one- and two-dimensional gel electrophoresis; peptide map identical with that of hepatic glucokinase after proteolysis with chymotrypsin and papain. These data indicate that the gene coding for hepatic glucokinase is expressed in RIN-m5F cells, a finding consistent with indirect evidence for the presence of glucokinase in the beta-cell of the islet of Langerhans. On the other hand, the overall pattern of hexokinases is distinctly different in RIN-m5F cells and islets of Langerhans, since hexokinase type II appears to be lacking in islets. Alteration in hexokinase expression after tumoral transformation has been reported in other systems.
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PMID:Hexokinase isoenzymes of RIN-m5F insulinoma cells. Expression of glucokinase gene in insulin-producing cells. 303 55

From poly(vinyl alcohol) precursors, various reactive carriers for the immobilization of enzymes were synthesized. As insoluble starting polymers, the following products were used: poly(vinyl alcohol), gels crosslinked with terephthalaldehyde, hydrolyzed beads of crosslinked poly(vinyl acetate), poly(vinyl acetate-co- ethylene) tubes coated with poly(vinyl alcohol), and poly(vinyl alcohol)-containing synthetic pulp. Reactive groups introduced into these carriers or methods for their activation included the diazonium- and isothiocyanato group, and the glutardialdehyde-, BrCN, 2, 4, 6-trichloro-s-triazien, and p-benzoquinone methods. Furthermore, SH-specific reactive groups such as N-substituted maleimide groups or activated mixed disulfides with 2-thiopyridyl groups could be introduced into PVA-polymers. Enzymes like hydrolases (e.g. papain, trypsin, chymotrypsin, urease), oxidoreductases (e.g. glucose oxydase, catalase, glucose-6-phosphate dehydrogenase) as well as the example of transferase hexokinase coimmobilized with glucose-6-phosphate dehydrogenase, were immobilized by reactive poly(vinyl alcohol) carriers. The properties of the immobilized enzymes were investigated.
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PMID:Some new reactive polymers for the immobilization of enzymes. 741 95

This report delineates scope and limitation of the selectivity of synthetic multifunctional pores as enzyme sensors using glycolytic enzymes as example (G. Das, P. Talukdar, and S. Matile, Science, 2002, Vol. 298, pp. 1600-1602). Unproblematic detectability of hexokinase and phosphofructokinase demonstrates that the selectivity of synthetic multifunctional pore (SMPs) sensors suffices to sense ATP in mixed analytes containing ADP, whereas detection of the isomerization of glucose 6-phosphate into fructose 6-phosphate by phosphoglucose isomerase is not possible with confidence. The sensitivity of SMP sensors is sufficient for end-point detection of one picomole poly-L-glutamate hydrolyzed by papain in unoptimized assay format; the sensitivity of melittin as representative biological pore of similar charge and aggregation number to detect the same reaction is more than four orders of magnitude inferior.
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PMID:On selectivity and sensitivity of synthetic multifunctional pores as enzyme sensors: discrimination between ATP and ADP and comparison with biological pores. 1499 75