Chicken lens delta-crystallin gene expression and methylation in several non-lens tissues.

RNA sequences coding for the most abundant chicken lens proteins, delta-crystallin, were detected at very low levels in day old post hatch chick lung, heart, kidney and liver, and in 6 day embryo headless bodies. The pattern of cytosine methylation within the CCGG sequences of the delta-crystallin genes was also examined and shown to vary in several non-lens tissues, from several stages of development. Embryonic neural retina, which expresses a higher level of delta-crystallin RNA than the above tissues, is no less methylated in the sites studied than the tissues which have no association with the eye, and is actually more heavily methylated than the kidney. Thus no obvious correlation was found between undermethylation and gene expression.     

Induction of the allantoin degradative enzymes by allophanic acid, the last intermediate of the pathway

$\text{Saccharomyces cerevisiae}$ can utilize allantoin as a sole nitrogen source by degrading it in five steps to ammonia, “CO₂”, and glyoxylate. We have previously shown that allophanic acid is the inducer of the urea carboxylase: allophanate hydrolase multienzyme complex. Since these enzymes catalyse the last two steps of allantoin degradation, experiments were performed to determine if allophanate was also the inducer of any other enzymes in the pathway. Our data demonstrate that allophanate induces synthesis of at least five of the seven purine degradative enzymes.     

Map location of arginyl-tRNA synthetase mutations in Escherichia coli K-12

Summary Mutants of Escherichia coli K-12 previously isolated in the authors' laboratory have reduced arginyl-tRNA synthetase activity. The mutants fall into two classes. All mutants grow slowly on arginine-free medium. On arginine-supplemented medium some mutants grow at a normal rate (Class I) while others still grow slowly (Class II). Matings were performed to located a Class I and a Class II mutation on the E. coli chromosome map, and on the basis of our results we have assigned both to one locus, argS.     

Sudden Failure of Swimming in Cold Water

To investigate the effect of cold water on swimming four men who declared themselves good swimmers were immersed fully clothed on separate days in water at 23·7° and 4·7° C. The time that they were able to swim in the cold water was much shorter than in the warm. The two shortest swims ended after 1·5 and 7·6 minutes, before rectal temperature fell, when the men suddenly floundered after developing respiratory distress with breathing rates of 56–60/min. The other cold swims, by the two fattest men, ended less abruptly with signs of general and peripheral hypothermia.It is concluded that swimming in cold water was stopped partly by respiratory reflexes in the thin men and hypothermia in the fat, and partly by the cold water''s high viscosity. The longer swimming times of the fat men are attributed largely to their greater buoyancy enabling them to keep their heads above water during the early hyperventilation.The findings explain some reports of sudden death in cold water. It is clearly highly dangerous to attempt to swim short distances to shore without a life-jacket in water near 0° C.     

On the site of action of phosphatide acyl-hydrolase activity of rat brain homogenates on lecithin

The hydrolysis of 2- [14C]acyl-labelled and [Me-3H]choline-labelled lecithins by rat brain homogenates has been studied. The acyl-labelled substrate was hydrolysed with the production of both radioactive lysolecithin and radioactive free fatty acid in the proportions of 60 per cent and 40 per cent; traces of labelled mono- and diglyceride were also formed. In addition to radioactive lysolecithin the [3H]choline-labelled lecithin also gave rise to much smaller amounts of radioactive water soluble derivatives, consisting almost entirely of free choline and phosphorylcholine with only traces of glycerylphosphorylcholine. The results provide evidence for the production of a mixture of 1- and 2-acyl isomers of lysolecithin by phospholipase action in brain homogenates at pH 7.4, the latter predominating slightly.