1. Exposure of submitochondrial particles to phospholipases impaired the rate of oxidation as well as phosphorylation. Phospholipase A and phospholipase C were more inhibitory to phosphorylation and to NADH oxidation than to succinate oxidation. 2. At low concentrations of phospholipase A the inhibition of phosphorylation was prevented to a considerable extent by the presence of large amounts o...

Rabbit antibody specific to the 2-azofluorenyl group (anti2-AzF antibody) was used to investigate the behavior of cellular components capable of binding 2-acetylaminofluorene (2-AAF) in rat livers during the chemical carcinogenesis. The fixation of the anti-2-AzP antibody in vitro by liver sec tions of rats fed or injected with fluorenyl derivatives was quan titatively measured by the radioiodi...

Myelin membranes prepared from rat brain possess both the enzyme and substrates to incorporate azP from (ya2P]ATP into membrane protein constituents. Qf the myelin polypeptides, only the two basic proteins were phosphorylated ; and both components appeared to be equally good substrates for endogenous or added protein kinases. The a2P was transferred primarily to serine residues of the basic pro...

We explore F.Jaeger’s state model for the HOMFLYPT polynomial. Reformulated in the language of Gauss diagrams it admits an elementary proof of existence of two HOMFLYPT polynomials for virtual string links which coincide in the case of classical links. In particular, for classical knots it gives a combinatorial proof of existence of the HOMFLYPT polynomial. In the second part of the paper we ob...

The phosphorylation of specific membrane proteins by endogenous protein kinase in synaptic membrane fractions from rat cerebrum has been studied using the technique of acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The endogenous phosphorylation of two specific membrane proteins was found to be regulated by adenosine 3’ : 5’-monophosphate (cyclic AMP). The minimal mol...

Escherichia co2i formylmethionine tRNA is unable to form a ternary complex with bacterial T factor and GTP, as measured by Sephadex G-50 gel filtration. Treatment of tRNAfMet with sodium bisulfite produces cytidine to uridine base changes in the tRNA structure and greatly enhances its binding affinity for T factor. The ternary complex formed with the bisulfite-modified initiator tRNA has proper...