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Biomedical subjects

R J Watson

Publications and source records attributed to R J Watson.

At least 109 records · Page 6Linked to original sources
PubMed1977

A large-scale professionally oriented medical information system--five years later.

Success is the word used most often to describe El Camino Hospital's computerized medical information system. Operational since 1972, the system has gained total support from virtually all hospital personnel. Physicians, nurses, and administrative people use the system routinely as part of their day-to-day activities. HEW-sponsored studies have heralded the system for its impact on improving patient care and containing costs. The following paper is an overview of the system from installation to the present. It tells of the vast information available to hospital professionals through simple lightpen selections on a CRT screen, how it handles most manual activities, how it reduces errors, and how it replaces the nurses' Kardex files. Automated systems technology is vital to the future of health care, and it is a valuable tool for enhancing the quality of patient care and improving the use of labor resources. This paper further gives an important insight into other benefits offered to all hospitals by the advent of systems such as the one at El Camino.

Attitude of Health Personnel↗
PubMed1976

A transducing bacteriophage lambda carrying the structural gene for elongation factor Ts.

A specialized transducing bacteriophage lambdadpolCdap D-9 has been isolated that carries the structural gene for EF-Ts1 (tsf). The presence of EF-Ts among the proteins synthesized under the direction of this phage in UVL-inactivated cells has been detected by two-dimensional gel electrophoresis and has been verified by antibody precipitation. In an induced lysogen of this phage the relative rate of synthesis of EF-Ts is increased 4-fold. Evidence is presented which suggest that the structural genes for ribosomal protein S2 (rpsB) and RNA polymerase sigma factor (sit) also lies on lambdadpolCdap D-9.

Coliphages↗
PubMed1976

A relaxed mutant with an altered ribosomal protein L11.

Relaxed mutants of Escherichia coli have been isolated which have an altered electrophoretic mobility of ribosomal protein L11. It can be shown that reversion to stringency in one of these mutants occurs simultaneously with a reversion of L11 protein to tis normal mobility. The L11 structural gene, rplK, maping near rif, is carried by the bacteriophage lambdacI857S7drifd18, and is most likely identical with relC.

Bacterial Proteins↗
PubMed1976

Isolation of transducing phage carrying rps T, the structural gene for ribosomal protein S20.

Lambda transducing phages carrying segments of the Escherichia coli chromosome in the dapB region have been isolated in their in vivo gene products analyzed by two-dimensional gel electrophoresis. One of these phages, lambdaddapB-2, carries the structural genes for ribosomal protein S20 (rps T) and isoleucyltransfer RNA synthetase (ileS.) The most likely gene order is thr-rpsT-ileS-dapB-pyrA.

Bacterial Proteins↗
PubMed1976

Isolation of a lambda transducing bacteriophage carrying the relA gene of Escherichia coli.

In Escherichia coli the relA and pyrG loci are 99% cotransducible. On the basis of this knowledge, we have isolated lambdacI857S7dpyrG transducing bacteriophages carrying both the pyrG and relA genes. Single lysogens of this bacteriophage show basal levels of ppGpp that are 10-fold higher than normal. Stringent factor is present among the gene products synthesized by lambdadpyrG relA after infection of ultraviolet-killed cells, as analyzed by polyacrylamide gel electrophoresis. The intracellular content of stringent factor, as determined by enzymatic activity, rises 20-fold after induction of a single lysogen of lambdadpyrG relA. As measured by two-dimensional gel electrophoresis, the amount of stringent factor in an exponentially growing strain carrying a pyrG relA plasmid is at least 10-fold greater than in a normal strain. These data constitute strong evidence that stringent factor is the relA gene product.

Amino Acids↗
PubMed1975

New chromosomal location for structural genes of ribosomal proteins.

An Escherichia coli mutant, ts9, previously reported by Flaks et al. (Cold Spring Harbor Symp. Quant. Biol. 31, 623-631, 1966) to have an electrophoretically altered ribosomal protein, has been further characterized and the altered component has been identified as L7/L12. Although mutant ts9 is temperature sensitive for growth (rts-), the rts and L7/L12 mutations are genetically separable and are both located between argH and rif. The L7/L12 mutation (rpyL) maps very close to relC, mutants of which have a defect in the 50S ribosomal subunit. The gene order is argH-rts-(rpyL,relC)-rif. Protein synthesis directed by bacteriophage lambdacI857S7drifd18 in ultraviolet-irradiated cells indicates that L7/L12, As well as L1, L10, L11, and possibly L8 or L9 are coded by the phage DNA. Our results indicate that rpyL is the structural gene for L7/L12 and that this region of the E. coli chromosome contains a cluster of structural genes for ribosomal proteins.

Bacterial Proteins↗
PubMed1972

Effect of shaking speed on the secretion of enterotoxin B by Staphylococcus aureus.

The concentration of enterotoxin B secreted by four strains of Staphylococcus aureus was dependent upon the shaking speed. For the conditions established, each strain demonstrated an optimal shaking speed, and speeds in excess of the optimum resulted in decreased secretion of toxin. At the optimal shaking speed, maximum secretion occurred at 37 C. At 45 C, both growth and toxin secretion were absent. By using agar containing antienterotoxin B sera, studies with strain S-6 at optimal and suboptimal shaking speeds demonstrated that individual cells vary in their toxin-synthesizing ability and that the relative numbers of high and low producers change during the growth cycle. Although most of the toxin was secreted during the first 12 hr of growth, a portion was secreted during the subsequent 6 hr, even though growth as measured by colony-forming units per milliliter decreased and Klett units increased.

Agar↗