The spatial heterogeneity of myocardial perfusion and metabolism was studied in 11 anaesthetized dogs under resting conditions. In each heart local myocardial blood flow was assessed using the tracer microsphere technique in 256 samples (mean mass: 83.1 mg) taken from the left anterior ventricular wall. In the same samples, the following biochemical parameters were determined: accumulation of [3H]-deoxyglucose (a measure of glucose uptake), free cytosolic adenosine (S-adenosylhomocysteine accumulation technique, a measure of tissue oxygenation and a possible mediator of blood flow regulation), and the specific activities of oxidative (citrate synthase, cytochrome-c-oxidase) and glycolytic (hexokinase, phosphoglycerate kinase) enzymes. Capillary density and mitochondrial and myofibril volume densities were determined by morphometry. Myocardial perfusion in each sample (average 0.77 ml min-1 g-1) varied between 0.1 and 2.5 times the mean (coefficient of variation 0.30+/-0.02). [3H]-deoxyglucose was deposited locally in proportion to perfusion. Samples showing low flow (<0.2 ml min-1 g-1) did not exhibit increased levels of cytosolic adenosine. The specific activities of the oxidative and glycolytic enzymes, however, were uniformly distributed between low and high flow areas. Furthermore, capillary density and mitochondrial and myofibril densities were similar in high and low flow regions. The results show firstly that local glucose metabolism in the heart occurs in proportion to local blood flow, suggesting that high flow regions have a higher than average metabolic rate. Secondly, regions of low flow are not compromized by critical oxygenation and most likely have a lower than average oxygen demand and finally, the homogeneous distribution of oxidative and glycolytic enzymes, as well as the homogeneous myocardial ultrastructure, suggest that areas with high and low blood flow under resting conditions may increase their metabolic rate to similar levels when required.

In the isolated perfused rat liver, both 5-aminolevulinate synthetase and tyrosine aminotransferase were induced by the addition of 3.5 mmol/l allylisopropylacetamide and 58 μmol/l dexamethasone to the perfusion medium. Glucose (40 mmol/l) did not affect either the induction of these enzymes or the intrahepatic level of cyclic AMP. The results suggest that the glucose effect on the induction of 5-aminolevulinate synthetase and tyrosine aminotransferase in vivo is mediated by extrahepatic factors.

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SYNOPSIS. A partially purified hexokinase extracted from Euglena had the following properties: 1) pH optimum 8.0–8.5; 2) an absolute requirement for Mg++ and adenosine triphosphate with Mn++, Co++, Zn++, and Ca++ less active or inactive under the test conditions. Inosine triphosphate could not be substituted for adenosine triphosphate; 3) an apparent Km (glucose) of 5 × 10−4 M; 4) the enzyme was not inhibited by the usual sulfhydryl agents, but was inhibited 24% by adenosine diphosphate. The extract phosphorylated fructose and mannose. It was not clear whether a separate enzyme phosphorylated fructose. Relative rates of phosphorylation, as determined by labile phosphate analyses, were: glucose, 1.00; fructose, 1.19; mannose, 0.56. The partially purified extract also contained phosphohexose isomerase activity; 6‐phosphogluconic acid dehydrogenase was absent. Euglena hexokinase is apparently localized in the cytoplasmic or small‐particle fraction of the cell. In most respects the enzyme seems to resemble the well‐characterized yeast hexokinase rather than the muscle enzyme.