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D P Leader

Publications and source records attributed to D P Leader.

80 records · Page 5Linked to original sources
PubMed1971

Aminoacyltransferase I-catalysed binding of phenylalanyl-transfer ribonucleic acid to muscle ribosomes from normal and diabetic rats.

The aminoacyltransferase I-catalysed binding of phenylalanyl-tRNA (unfractionated Escherichia coli B tRNA acylated with radioactive phenylalanine and 19 non-radioactive amino acids) to skeletal-muscle ribosomes from diabetic rats was less than that to ribosomes from normal rats when the Mg(2+) concentration was low (7.5mm); whereas just the reverse was true when the concentration of the cation was higher (15mm). Thus the Mg(2+) dependency of aminoacyltransferase I-catalysed binding of phenylalanyl-tRNA to ribosomes from normal and diabetic rats paralleled the effect of Mg(2+) concentration on synthesis of polyphenylalanine reported before. During incubation at 7.5mm-Mg(2+) phenylalanyl-tRNA was bound only to ribosomes bearing nascent peptidyl-tRNA. There are fewer such ribosomes in a preparation from the muscle of diabetic animals because diabetic animals synthesize less protein in vivo. Thus the difference in polyphenylalanine synthesis in vitro is adequately explained by the difference in enzyme-catalysed binding of phenylalanyl-tRNA to ribosomes, however, the basis of the difference in protein synthesis in vivo is still unknown.

Acyltransferases↗
PubMed1970

A factor for the binding of aminoacyl transfer RNA to mammalian 40S ribosomal subunits.

A factor present in rat liver supernatant catalyzes binding of Phe-tRNA to 40S ribosomal subunits from rat skeletal muscle. This factor could be distinguished from aminoacyltransferase I by a number of criteria: (1) at lower concentrations of magnesium (5 mM) the 40S binding factor was approximately seven times as effective as T-I in catalyzing binding of Phe-tRNA to 40S subunits; (2) the kinetics of the binding reaction were different when catalyzed by the 40S binding factor, in particular the initial rate was greater than in the presence of T-I-indeed, the kinetics of the T-I catalyzed reaction resembled nonenzymic binding; (3) GTP was required for maximal binding of Phe-tRNA to 40S subunits in the presence of the 40S binding factor, but not for the T-I catalyzed reaction; (4) the 40S binding factor was inactivated by N-ethylmaleimide whereas T-I was not; (5) finally, the 40S binding factor was more susceptible to heat inactivation. Binding of aminoacyl-tRNA to 40S ribosomal subunits may be a paradigm for the initiation of protein synthesis, and the 40S binding factor may play a role in the process.

Acyltransferases↗
PubMed1969

Increase in activity of glucose 6-phosphate dehydrogenase in mouse mammary tissue cultured in insulin.

1. In organ cultures of mammary tissue from C3H mice we observed increases in the activity of glucose 6-phosphate dehydrogenase similar to that occurring at parturition. 2. In 22hr. cultures of tissue from late-pregnant mice insulin was required for the increases, but the further addition of prolactin, corticosterone and certain other hormones had no effect. The rise in activity occurred over the second half of the culture period. 3. Results from culture of adipose tissue, and mammary tissue rich in adipose tissue, strongly suggest that the rise in activity occurs in mammary parenchymal rather than adipose cells. 4. In 45hr. cultures prolactin prevented a fall in enzyme activity between 22hr. and 45hr. If the medium contained serum the activity at 22hr. was unaffected, but it continued to rise up to 45hr., and prolactin then had no effect. 5. The enzyme also increased in activity in cultures of mammary tissue from mid-pregnant mice. Insulin was again required, the activity was higher at 45hr. than at 24hr. and prolactin increased the activities at both these times. 6. Actinomycin D, cycloheximide and puromycin at low concentration in the media of 22hr. cultures all prevented increases in enzyme activity. Hydroxyurea at a concentration that inhibited the incorporation of [(3)H]thymidine into DNA by 92% had little effect. 7. Actinomycin D and cycloheximide largely failed to prevent the rise in enzyme activity if added after 3.5hr. and 12hr. respectively. Hence all essential RNA and protein synthesis appears to be finished by 3.5hr. and 12hr., although most of the increase in enzyme activity occurs gradually between 12hr. and 22hr. 8. We suggest that the increases in enzyme activity, both in culture and in the living animal at parturition, are induced by an influx of glucose that is restrained during pregnancy by the growth-hormone-like action of placental lactogen.

Adipose Tissue↗
PubMed1967

Physical and chemical reactions of phosphates in red cell membranes in relation to active transport.

1. A study has been made of the chemical reactions associated with the active transport of sodium and potassium in human red cells, with special reference to the action of oligomycin and the labelling of cell membranes by radioactive ATP.2. Oligomycin had the same effects as ouabain on the various aspects of active transport in red cells. It inhibited sodium and potassium transport, the transport ATPase, and the lactate production that is controlled by the sodium pump.3. When cell membranes were incubated with radioactive ATP they became labelled. The labelling, however, was unrelated to the activity of the transport ATPase. Incubation of membranes and intact cells showed that the labelling was a result of physical adsorption of inorganic phosphate to the membranes.4. The results show that if there is a phosphate intermediate in the reaction of the transport ATPase in human red cell membranes, then it is present in amounts too small to be detectable by the methods that have been successfully used with organs such as brain and kidney.

Adenosine Triphosphatases↗