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Biomedical subjects

H R Knull

Publications and source records attributed to H R Knull.

At least 37 records · Page 2Linked to original sources
PubMed1982

Glycogen metabolizing enzymes in brain.

Three enzymes, glycogen phosphorylase, glycogen synthase, and phosphoglucomutase were evaluated in subcellular fractions and in brain regions. Also the development of each of these enzymes was evaluated in whole brain homogenates. Each enzyme increased during the first three weeks of post partum in a manner that is similar to the development of glycolytic enzymes during this period. The specific activity of each enzyme in various subcellular fractions indicated that the enzymes were primarily soluble. Also unlike the glycolytic enzyme phosphoglycerate kinase, the glycogen metabolizing enzymes had a lower specific activity in synaptosomes than in particle free supernatant fractions of homogenates. Regarding regional distribution small (less than twofold) but significant differences were seen between different brain areas. An inverse relationship between the glycogen metabolizing enzymes and hexokinase was observed, that is, regions highest in glycogen synthase and glycogen phosphorylase were lowest in hexokinase and regions highest in hexokinase were lowest in the glycogen metabolizing enzymes.

Age Factors↗
PubMed1981

Interaction of muscle glycolytic enzymes with thin filament proteins.

Purified glycolytic enzymes were individually chromatographed through columns of Sepharose 4B containing a covalently bound F-actin-tropomyosin complex. Five of these enzymes, aldolase, glyceraldehyde-phosphate dehydrogenase, lactate dehydrogenase, pyruvate kinase, and phosphoglycerate kinase were able to interact with the complex. Glucosephosphate isomerase, triosephosphate isomerase, phosphoglycerate phosphomutase, and enolase did not bind to the F-actin-tropomyosin matrix. One nonbinding enzyme, phosphoglycerate phosphomutase, was observed to interact with F-actin-tropomyosin if the column was preloaded with lactate dehydrogenase. Since at least four other glycolytic enzymes did not associate with actin directly, it is suggested that if a glycolytic enzyme complex exists, these nonadsorbing enzymes must interact with one or more of the enzymes which do bind to actin.

Actins↗
PubMed1980

Compartmentation of glycolytic enzymes in nerve endings as determined by glutaraldehyde fixation.

Considerable amounts of five glycolytic enzymes glucosephosphate isomerase, glyceraldehyde-phosphate dehydrogenase, aldolase, pyruvate kinase, and lactate dehydrogenase, became fixed when intact synaptosomes were incubated with glutaraldehyde. Other glycolytic enzymes were immobilized much less by this procedure. The lactate dehydrogenase isoenzymes showed a variable response to glutaraldehyde fixation. The isoenzymes enriched in muscle subunits were rapidly immobilized by glutaraldehyde, while the isoenzymes enriched in heart subunits, especially H4, were not. It is suggested that the enzymes which were immobilized are located near the synaptosomal membrane, perhaps in association with actin, which is found at this site. The enzymes that showed a much smaller degree of fixation were either randomly distributed in the synaptoplasm or less susceptible to fixation.

Aldehydes↗
PubMed1978

Association of glycolytic enzymes with particulate fractions from nerve endings.

Several glycolytic enzymes were observed to have between 40-90% of their activities associated with the particulate fractions of lysed nerve endings. The enzymes showing high particulate activity in lysed nerve endings were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), glucosephosphate isomerase (EC 5.3.1.9), phosphofructokinase (EC 2.7.1.11), glyceraldehyde-phosphate dehydrogenase (EC 1.2.1.12), pyruvate kinase (EC 2.7.1.40) and lactate dehydrogenase (EC 1.1.27). With the exception of phosphofructokinase, 80% or more of the particle associated activity of each enzyme was solubilized by salt treatment indicating the association with particles was ionic. Sub-fractionation of lysed nerve endings showed hexokinase and fumarase (EC 4.2.1.2) had the highest specific activity in the same fractions which is consistent with observations indicating that hexokinase is associated with mitochondria. The other glycolytic zymes having high particulate activity, aldolase, glucosephosphate isomerase, phosphofructokinase, glyceraldehyde-phosphate dehydrogenase, pyruvate kinase and lactate dehydrogenase, showed enrichment in fractions containing synaptosomal membranes, i.e. the fractions having highest specific activity of acetylcholinesterase (EC 3.1.1.7) and (Na+ + K+)-ATPase (EC 3.6.1.3).

Adenosine Triphosphate↗
PubMed1975

Reversibility of mechanical and biochemical changes in smooth muscle due to anoxia and substrate depletion.

The effect of temporary glucose and oxygen deprivation on isometric tension as well as content of glycogen, creatine phosphate (CP), adenosine triphosphate (ATP), adenosine diphosphate (ADP), adenosine monophosphate (AMP), and adenylate pool (AP) were studied in potassium-contracted guinea pig isolated taenia coli. Under aerobic conditions glucose removal caused a decrease in tension, glycogen, CP, ATP, and energy charge; ADP and AMP increased, keeping the adenylate pool size unchanged. During rigor caused by additional anoxia, there was an increase in tension associated with further decrease in ATP and marked reduction of adenylate pool. Restoration of oxygen supply caused only a small increase in ATP that, though sufficient for abolishing rigor, was insufficient to support potassium contraction. Restoration of both glucose and oxygen did not restore tension even though ATP stores were increased further. Elevation of extracellular calcium caused partial restoration of tension, suggesting that the defect was in calcium metabolism rather than energy metabolism. During recovery AP remained low, possibly due to deamination of AMP. Anoxia in the presence of glucose reduced ATP to a concentration similar to that due to aerobic glucose deprivation but tension decreased much less. This result is consistent with different degrees of ATP depletion in various functional (Ca pump vs. contractile mechanism) compartments.

Adenosine Diphosphate↗