The social and economic milieu of health care provision: quality, access, and cost.
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Costs and Cost Analysis↗
Biomedical subjects
L E Jensen
Publications and source records attributed to L E Jensen.
Foreign medical graduates and the issue of substantial disruption of medical services.
Provisions of the 1976 Health Professions Educational Assistance Act may result in a substantial disruption of medical services provided by foreign medical graduates in United States residency training programs. Estimates of the effect of the Act indicate that between one third and two thirds of foreign graduates receiving visas annually will not qualify for admission, under the new provisions. Results of a recent study show, furthermore, that foreign medical graduates constitute a majority of the residents in 23 per cent of the hospitals with residency programs. Transition to a decreased dependence on foreign graduates may be facilitated through the waiver of two provisions relating to exchange visitors. Projected numbers of United States medical graduates and citizens receiving medical education abroad will not be enough to fill the gap created by the ultimate reduction in alien physicians. United States residency programs will have to develop alternative sources of residents to continue operating at current levels.
Delivery of Health Care↗
Toxicity of intravenous catheters tested in a human bone marrow culture system.
Nine brands of i.v. catheter were tested for toxicity in a human bone marrow culture system, and content and leaching of plasticizers determined. Three catheters showed toxicity to the culture system and three others leached di-2-ethylhexyl-phthalate in appreciable amounts.
Bone Marrow Cells↗
Isolation of a pentraxin-like protein from rainbow trout serum.
Serum amyloid P-component (SAP) is a glycoprotein consisting of five or ten noncovalently associated identical subunits of molecular weight 19,000-30,000. Herein we report the isolation and partial characterization of a SAP-like protein from rainbow trout serum. The protein was isolated by calcium-dependent binding to Sepharose followed by ion-exchange and size-exclusion chromatography. Rabbit antibody against human SAP reacted with the trout protein and the NH2-terminal sequence of 16 amino acids showed 60% identity with the first 15 residues of human SAP. SDS-PAGE and endoglycosidase treatment indicated that the trout protein is a glycoprotein in which five or six subunits are linked by disulphide bonds. The subunits have a molecular weight of 37,000 of which approximately 13% is due to carbohydrate. We propose to name the trout protein sulphide linked SAP (SL-SAP).
Alpha-Globulins↗