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Biomedical subjects

H Amos

Publications and source records attributed to H Amos.

52 records · Page 3Linked to original sources
PubMed1970

Ribonucleic acid synthesis and transport in animal cells at 27 degrees C.

The failure to induce glutamine synthetase in retinal cells with hydrocortisone at 27 degrees C (37 degrees C is the normal temperature for induction) led to a study of some aspects of RNA synthesis at 27 degrees C by using the method of selective labelling with radioactive precursors, sucrose-density-gradient centrifugation and radioautography. The low-temperature treatment not only decreases the rate of RNA synthesis but also interferes with the general pattern of RNA maturation and distribution. It has been found that nuclear-cytoplasmic exchange is severely altered at low temperature and may be an explanation of the failure to induce the enzyme. When the temperature is raised from 27 degrees C to 37 degrees C, the incorporation of exogenous radioactive uridine into the RNA is distorted by a pool-dilution effect that results in an ;over-shoot' phenomenon. The kinetics of labelled uridine equilibration into the UMP pool accounts for the difficulty encountered by many investigators in ;chase' efforts with unlabelled nucleosides.

Animals↗
PubMed1968

Hydrocortisone requirement for the induction of glutamine synthetase in chick-embryo retinas.

Hydrocortisone has been found to induce glutamine synthetase activity in chick-embryo retinas in culture. Evidence is presented to show that the hydrocortisone is definitely required for transcription; its requirement for translation has not been ruled out. The possible identity of hydrocortisone with an active component of calf-serum diffusate reported earlier is discussed. The data also indicate that the glutamine synthetase messenger RNA is stable for at least several hours.

Animals↗
PubMed1967

Protein synthesis in sonically damaged Escherichia coli.

By gentle sonic treatment, Escherichia coli cells were modified to permit penetration of actinomycin D, adenosine triphosphate, trypsin, ribonuclease, and polyuridylic acid. The behavior of these "soniplasts" as protein-synthesizing particles was investigated.

Adenosine Triphosphate↗
PubMed1966

Arrested protein synthesis in polysomes of cultured chick embryo cells.

Cells deprived of serum synthesize proteins at a reduced rate; when serum is restored the rate returns to normal. The polysomes do not dissociate, but show reduced incorporation of amino acid in vitro, and are less responsive to polyuridylic acid than are those from normal cells.

Animals↗
PubMedDate not supplied

A moral quandary for sponsors. Like the family, and the state, sponsorship is an institution.

Nowadays many religious institutes are asking questions about sponsorship. The issue is usually phrased as the sponsoring of institutions. But it might be useful to ask about the institution of sponsorship instead. In The Good Society, Robert Bellah and his associates say that, on one hand, institutions are created by human beings; on the other hand, because we draw our sense of identity from them, institutions create us too. Bellah et al. also say that institutions, being human creations, are susceptible to corruption, especially when great wealth and power are involved. Since hospitals and healthcare systems obviously do involve wealth and power, we sponsors now have many questions, as well as some ambiguity about our sponsorship capability. One might even say that a moral debate is raging in our collective subconscious: Is loss of corporate influence something we would do something about if we could, or have we chosen some other value, such as ministerial diversity, instead? My institute, the Sisters of Mercy, has decided to continue our sponsorship of such organizations. As an institution, sponsorship is an essential bearer of our ideals and meanings. We need this institution to announce, to the world and to ourselves, that whatever power and wealth we possess are committed to mercy and justice.

Catholicism↗