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D Stone

Publications and source records attributed to D Stone.

At least 163 records · Page 9Linked to original sources
PubMed1977

Professionalism and accountability. Controlling health services in the United States and West Germany.

This paper examines the new Professional Standards Review Organizations (PSROs) program in light of a similar program ("Economic Monitoring") that has been used in West Germany for over forty years. In the first section the PSRO program is described as government-mandated peer review by professional organizations, and is compared with that of the West Germany system. The second section argues that the PSROs are likely to strengthen the organization of established medicine, to increase the bargaining power of professional organizations, and to further insulate professional behavior from public scrutiny. The third section describes some of the effects of bureaucratic rigidities in peer review on the practice of medicine: the preservation of old technologies, the development of fixed patterns of practice, and the strengthening of the technical and interventionist biases in medical care. The final section evaluates the PSRO program as a complete delegation of congressional authority and a failure of Congress to set any rules for the development and application of norms and standards. The lack of any mechanism for accountability of the PSROs to public and choices is emphasized.

Delivery of Health Care↗
PubMed1976

Nine-one-one.

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Emergency Medical Services↗
PubMed1973

Studies on the heterogeneity of subfragment-1 preparations. Isolation of a new proteolytic fragment of the heavy chain of myosin.

1. The physical, chemical and enzymic properties of subfragment 1 prepared from myosin of rabbit skeletal muscle by using two different concentrations of insoluble papain were compared. 2. Subfragment 1 prepared by using a myosin/papain ratio of 2000: 1 (by wt.) migrated on electrophoresis in non-dissociating conditions as a single enzymically active band. When prepared with a myosin/papain ratio of 200: 1 the preparation consisted of two enzymically active components of slightly different electrophoretic mobility. 3. The two types of preparation were obtained in similar yield and possessed similar specific adenosine triphosphatase activities when determined in the presence of Ca(2+). 4. Gel electrophoresis in the presence of 8m-urea showed that both preparations contained three light components. The component of molecular weight 15500 was apparently identical with one of the light-chain components of myosin (Ml(1)). The other two light-chain components of subfragment 1 were not identical with any of the light-chain components of myosin. 5. The heavy-chain fraction of subfragment 1 prepared by using low concentrations of papain dissociated into components with molecular weights of 87000, 69000 and 26000 on electrophoresis in sodium dodecyl sulphate. The heavy-chain fraction of subfragment 1 prepared by using higher concentrations of papain contained components with molecular weights of 69000 and 53000 and relatively increased amounts of the component of molecular weight 26000. 6. The isolated 26000 dalton component had an amino acid composition similar to that of the heavy-chain fraction of subfragment 1 and contained 3-methylhistidine and mono-and tri-N(epsilon)-methyl-lysine. It was homogeneous on electrophoresis in the presence of sodium dodecyl sulphate but gave two bands on electrophoresis in 8m-urea.

Adenosine Triphosphatases↗
PubMed1972

Possibility of in vitro alterations in cultures of mammary carcinoma cells, and altered immunological response in the rat: acquired capacity to reject injections of mammary carcinoma cells and implants of mammary carcinoma.

Cell cultures derived from a mammary adenocarcinoma carried in inbred Fisher (CDF) strain female rats, have been shown to possess oncogenic activities and on injection into control rats to produce mammary carcinomata with a failure rate of only one out of 25 rats (i.e. 4%). Efforts have been made to alter the cultured cells, or to select populations from them, so that the response in rats to their antigenic characteristics might leave them with the ability to then reject injections of the active, untreated cancer cells. We have found that continuous treatment of the cultures by their own cell debris (sonicate), or by relatively high concentrations of intact, salmon-sperm DNA, lead to cell populations which have a decreased potential to produce mammary carcinomata, with a combined failure rate of 9 out of 12 rats (i.e. 75%): 5 out of these 12 rats (i.e. 41·7%) did not exhibit any growth (carcinomata or granulomata) after injection of these treated cells, and now all 5 (i.e. 100%) have the capacity to reject injections of the untreated, active cancer cells. Four of these rats (one died under anaesthesia) have now been found to also reject implants of the carcinoma itself.

Adenocarcinoma↗
PubMed1970

Occurrence and formation of the N epsilon-methyl-lysines in myosin and the myofibrillar proteins.

1. Adult rabbit skeletal-muscle myosin has been shown to contain 1.0 residue of mono-N(in)-methyl-lysine and 3.3 residues of tri-N(in)-methyl-lysine per molecule of molecular weight 500000. 2. The methyl-lysines appear to be located in the subfragment 1 portion of the myosin molecule. 3. Methyl-lysines are not present in actin, tropomyosin, inhibitory factor and calcium-sensitizing factor. 4. Enzymic methylation of histidine and lysine residues of myosin has been demonstrated in vitro. 5. The methylation of histidine and lysine of the total myofibrillar protein occurs after peptide-bond synthesis. 6. Although methylated lysines and 3-methyl-histidine could not be detected by analysis of hydrolysates, radiochemical evidence is provided for the presence of these residues in the soluble-protein fraction of rabbit skeletal muscle.

Amino Acids↗