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Biomedical subjects

K Mayer

Publications and source records attributed to K Mayer.

At least 199 records · Page 11Linked to original sources
PubMed1975

[Computer experience and further developments in the respiratory function laboratory (author's transl)].

Reported is on satisfactory results obtained with a small-size computer consisting of punching and scanning device, as well as plain writing machine in the respiratory function laboratory. Developed in on- as well as off-line processing by an own technical staff, a diagnostic and teaching program was established for all respiratory function routine methods with the advantages of a large number of cases examined, elimination of sources of error, considerable supply of data and information, automatic documentation and filing, plain writing, interpretation and evaluation of findings. In continuation of such works also the blood gas analysis has been included. These values as the total of disturbances of the pathophysiological acid-base status are considered and interpreted. Clinical correction is forced in this man-machine dialogue by automatic stops of the whole machinery before going on. Subsequently and in addition are computer alveolar-arterial oxygen pressure gradient, venous shunt and oxygen saturation and expressed utilizing the capacity of the small-size computer. Further developments in the respiratory function diagnostic- and teaching program for small-size computers--not too expensive in the building block principle - are intended.

Acid-Base Equilibrium↗
PubMed1975

[An acid-base blood-gas calculator (author's transl)].

A prerequisite for the practical application of the blood-gas values is a calculation of the base excess with regard to the Hb and the interpretation of the acid-base status present. We have provided an aid for the rapid and practicable carrying out of calculations, based on well known nomograms and we think it gives, in principle, a simplification of the method.

Acid-Base Equilibrium↗
PubMed1975

[Representative enzymes of energy supplying metabolism in the normal and denervated human brachial biceps, deltoid and anterior tibial muscles (author's transl)].

Representative enzyme activities of energy supplying metabolism were measured in muscle specimens of brachial biceps, deltoid or anterior tibial muscle of patients with affections of the peripheral nerves. Simultaneously performed measurements of the same enzyme activities in the contralateral normal muscles served as a control. 5 patients suffered from a lesion of the brachial plexus, 7 patients had a paralysis of the axillary nerve, and 8 patients had a peroneal paralysis. In all denervated muscles no electrophysiological signs of reinnervation were present. The activities of glycogen phosphorylase, triosephosphate dehydrogenase, lactate dehydrogenase and alpha-glycerophosphate dehydrogenase were found to be highest in the normal brachial biceps muscle. Lower activities were measured in the normal deltoid and anterior tibial muscle. The oxidative enzymes, 3-hydroxyacyl-CoA dehydrogenase and citrate synthase as well as hexokinase, showed no significant difference from the levels of the control. It is suggested that a probable factor determining the differences of the enzyme activities of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation between brachial biceps, deltoid and anterior tibial muscle, might be the pattern of impulse activity in the motor nerves of these muscles. The enzyme activities of glycogen phosphorylase, triosephosphate dehydrogenase, lactate dehydrogenase and alpha-glycerophosphate dehydrogenase, decreased rapidly during the first 2 months after denervation in the brachial biceps, deltoid and anterior tibial muscle, whereas the decrease was slight during the following months. The activities of the oxidative enzymes (3-hydroxyacyl-CoA dehydrogenase and citrate synthase) showed no significant change after denervation. The metabolic difference of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation between the three muscles was no longer maintained. The possible causes of the deeply decreased enzyme activities of glycogenolysis, glycolysis and alpha-glycerophosphate oxidation, as well as the causes of the unchanged oxidative enzyme activities and of the increased hexokinase activity after denervation in the human brachial biceps, deltoid and anterior tibial muscle, are discussed.

Adolescent↗
PubMed1975

On the mechanism of action of isocitrate lyase.

1. The enzymes citrate lyase and isocitrate lyase catalyse similar reactions in the cleavage of citrate to acetate plus oxaloacetate and of isocitrate to succinate plus glyoxylate, respectively. 2. Nevertheless, the mechanism of action of each enzyme appears to be different from each other. Citrate lyase is an acyl carrier protein-containing enzyme complex whereas isocitrate lyase is not. The active form of citrate lyase is an acetyl-S-enzyme but that of isocitrate lyase is not a corresponding succinyl-S-enzyme. 3. In contrast to citrate lyase, the isocitrate enzyme is not inhibited by hydroxylamine nor does it acquire label if treated with appropriately labelled radioactive substrate. 4. Isotopic exchange experiments performed in H18-2O with isocitrate as a substrate produced no labelling in the product succinate. This was shown by mass-spectrometric analysis. 5. The conclusion drawn from these results is that no activation of succinate takes place on the enzyme through transient formation of succinic anhydride or a covalently-linked succinyl-enzyme, derived from this anhydride.

ATP Citrate (pro-S)-Lyase↗
PubMed1974

Mapping human autosomes: evidence supporting assignment of rhesus to the short arm of chromosome No. 1.

Rh-negative erythrocytes were found in the blood of an Rh-positive man suffering from myelofibrosis. Nucleated hemopoietic precursors were also circulating in his blood, and these cells had an abnormal chromosome complement from which identifiable chromosome segments had been deleted. Correlation of the serological and cytogenetic findings, combined with previous data, indicates that the Rhesus blood group locus is on the distal portion of the short arm of chromosome No. 1.

Chromosome Aberrations↗