Protein phosphorylation in a dopamine-sensitive homogenate of rat caudate: Effect of adenosine 3′,5′-cyclic monophosphate and putative neurotransmitters

Adenosine 3′,5′-cyclic monophosphate (cyclic AMP) and its 8-methylthio derivative stimulate the incorporation of ³²P into proteins endogenous to a homogenate of rat caudate nucleus when 4 μM [γ?³²P] ATP is usedas substrate. Higher concentrations of ATP reduced the effect of the cyclic nucleotide until at 400 μM no significant increase in protein phosphorylation was seen.Incubation of the homogenate with 400 μM ATP and 100 μM dopamine resulted in an approx. 2-fold increase in cyclic AMP but did not alter caudate protein phosphorylation suggesting that the catecholamine could not stimulate protein phosphorylation under the experimental conditions used in the present study.     

Northern Health Service in Canada

The current state and future development of Canada''s North present significant medical problems. The medical facilities available at present are inadequate and, although they are improving rapidly, they must keep pace with the coming expansion of the North. Arctic regions of other northern countries do not show the great discrepancies in health standards that Canada''s North does in comparison to her southern areas. To improve the situation adequate communication, transportation, personnel and facilities are needed. It is proposed that residents in hospital training programs work for a period in the North to supplement recommendations of the Hall Commission in this connection and to broaden their own training.     

Outgrowth promoting factor for the inner cell mass of the mouse blastocyst

When cultured individually, isolated inner cell masses (ICMs) of the mouse blastocyst form an outer layer of endoderm and remain in suspension as spherical structures for several days. Conditioned media from certain teratocarcinoma- and blastocyst-derived cell lines contain one or more outgrowth promoting factors (OPF) which facilitate attachment and outgrowth of ICMs, in some cases prior to endoderm formation. OPF adheres to culture dishes and presumably promotes ICM cell outgrowth by alteration of the substratum. Analyses indicate that the active material is a nondialyzable protein which is stable to freezing and thawing, a wide range of pH, and extended incubation at 37°C. However, inactivation takes place at 60°C for 20 min. Although these properties of OPF are in some ways similar to those of various proteins which have been implicated in cell adhesion and spreading, differences between OPF and most of these other proteins are evident. The detection of OPF activity in conditioned medium from primary cultures of embryonic and some extraembryonic cell types suggests that the factor is biologically significant, perhaps, for example, in the spreading of parietal endoderm cells along the surface of the trophoblast layer.     

The independent distribution of amino acid near neighbor pairs into polypeptides

With the assumption that individual amino acids are independently distributed into naturally occurring polypeptide chains, it is shown that amino acid pairs with 0–2 arbitrary intervening residues are also independently distributed, with a few possible exceptions. This is not true of N- and C-terminal amino acids.