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.     

The fine structure of the sieve tubes of Salix caprea (L.) and its relation to the electroosmotic theory

Summary The sieve plate pores of Salix caprea in preparations fixed in glutaraldehyde are normally found to be occupied by slime fibrils showing periodic banding such as occur in a number of other species. Arguments are put forward to suggest that the occurence of fibrils in this position is natural and not an artefact of preparation. The sieve tubes further possess prominent and persistent nucleoli showing a radiating structure of tubules. The endoplasmic reticulum often occurs in parietal stacks reminiscent of other species.This evidence is discussed in relation to the electroosmotic theory of translocation.This work formed part of that submitted for the degree of Ph. D. of the University of London by U. Mishra.     

Column chromatography of human small-intestinal maltase, isomaltase and invertase activities

1. The maltase, isomaltase and invertase (sucrase) activities of solubilized mucosal preparations from human jejunum and ileum were studied with column chromatography on anion-exchange (diethylaminoethyl- and triethylaminoethyl-)cellulose and Sephadex G-200 gel. 2. On ion-exchange cellulose columns both kinds of enzyme preparations yielded two major disaccharidase peaks. The first peak contained maltase Ia (=isomaltase) and maltase Ib (=invertase). The second peak contained maltase II and maltase III. 3. On Sephadex G-200 gel columns jejunal preparations yielded the corresponding peaks as on ion-exchange columns, but the peaks appeared in the reverse order in the effluent. The ileal preparation studied yielded a single peak on gel columns, containing all the activities studied and eluted with the `void volume'. 4. Precipitation with ethanol did not affect the behaviour of the enzymes during ion-exchange chromatography. When gel filtration was performed after ethanol precipitation of the enzymes, however, two peaks were obtained also with the ileal preparation, and subfractionation of the invertase was obtained with both kinds of preparations. 5. The second peak from ion-exchange chromatograms, containing maltase II and maltase III, on concentration was found to have very weak isomaltase activity, probably exerted by these enzymes as such. This activity accounts for only about 1% of the total isomaltase activity of the mucosa. 6. The results support the concept of the specificity of the human small-intestinal disaccharidases previously described after heat-inactivation experiments. The subfractionation of the invertase that under certain conditions is seen on Sephadex G-200 columns appears most likely to be an artifact. Consequently the nomenclature for the human maltose-, isomaltose- and sucrose-splitting enzymes proposed by another research group after gel-filtration chromatography studies should be abandoned. It seems more logical to keep the nomenclature based on heat inactivation [maltase Ia (=isomaltase), maltase Ib (=invertase or sucrase), maltase II and maltase III] until increased knowledge about the specificity and structure of these enzymes makes possible a more rational nomenclature.