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Biomedical subjects

J I Sandson

Publications and source records attributed to J I Sandson.

10 recordsLinked to original sources
PubMed1981

Rheumatology education in United States medical school.

Although rheumatology manpower in United States medical schools has dramatically increased in the past decade, 13% of medical schools did not have a full-time staff rheumatologist in 1980. Thirty-eight percent of medical schools had 2 or less full-time rheumatologists. Staff rheumatologists and rheumatology fellows provided the majority of medical student education in the clinical aspects of rheumatic disease; however, rheumatologists in less than 50% of medical schools taught in the basic science curriculum or in related fields such as collagen biochemistry, metabolic bone disease, and orthopedic intervention in arthritis. The staff rheumatologists' time commitment to medical student education was inversely proportional to the rheumatology faculty size. At medical schools with no rheumatologists, however, there was little, if any, formal education in the rheumatic diseases. Most subjects are taught in systems-oriented lectures. Education is currently limited to the common rheumatic conditions such as bursitis and back pain. Only 62% of medical schools provide a structured course on the musculoskeletal examination. Elective rotations in rheumatology, usually offered in the third or fourth year, are currently being provided to only 15% of U.S. medical students.

Curriculum↗
PubMed1972

Immunochemistry of cartilage proteoglycan. Immunodiffusion and gel-electrophoretic studies.

Cartilage proteoglycan is thought to be composed of subunits, core proteins with covalently attached sulphated polysaccharide side chains, which form aggregates by non-covalent association with a link protein. The new technique of non-disruptive extraction followed by fractionation in caesium chloride gradients provides a useful means of preparing relatively pure proteoglycan aggregate, subunit and link fractions. Immunological studies of these fractions led to the identification of an antigen associated with the proteoglycan subunit which was common to several species and to the demonstration of additional species-specific antigens in aggregate and link fractions derived from bovine nasal cartilage. Polyacrylamide-gel electrophoresis with sodium dodecyl sulphate of bovine proteoglycan aggregate and link fractions gave two protein bands in the gels and a protein-polysaccharide band at the origin; subunit fractions gave only the band at the origin. These results are consistent with the current concept of cartilage proteoglycan structure.

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