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Biomedical subjects

M Boesman

Publications and source records attributed to M Boesman.

15 recordsLinked to original sources
PubMed1968

Plasma 3S gamma-1-globulin: identity with erythrocyte carbonic anhydrase B.

The 3S (gamma1), 2S (gamma2), and 0.5S (gamma2) fractions of human plasma are heterogeneous in protein composition. Although each fraction contained a relatively small amount of protein antigenically related to the immunoglobulin light chains, most of the proteins were unrelated to immunogloublin G or its light chains. Of the 3S (gamma1)-globulins the greater part was immunochemically identical to carbonic anhydrase B and had carbonic anhydrase activity. These findings explain earlier reports of an immunochemical similarity between 3S (gamma1)-globulins and immunoglobulin light chains in spite of marked differences in amino acid and peptide composition between the two. Apparently not all plasma gamma-globulins are necessarily immunoglobulins.

Carbonic Anhydrases↗
PubMed1967

Passive transfer of tuberculin reactivity in vitro.

A factor capable of effecting passive transfer in vivo of delayed hypersensitivity to tuberculin to recipients that are tuberculin negative was isolated from the dialyzate of disrupted leukocytes of tuberculin-positive individuals. After this factor was incubated with cultures of peripheral leukocytes from tuberculin-negative individuals, the addition of purified protein derivative of tubercle bacilli resulted in leukocyte stimulation similar to that observed after addition of purified protein derivative to leukocytes from tuberculin-positive individuals.

Bacterial Proteins↗
PubMed1967

Sites of serum alpha-fetoprotein synthesis in the human and in the rat.

Selected tissues from human embryos of 6 to 9 weeks' gestation, from rat fetuses of 15 days' gestation, and from rats 2 days of age were incubated with (14)C-labeled amino acids. Immunoelectrophoresis of the culture fluid after incubation, using rabbit antisera against human and rat fetal serum proteins, followed by radioautography revealed that: 1) Radioactive alpha-fetoprotein was present in cultures of human liver, rat liver, and rat yolk sac, but not in cultures of human or rat brain, lung, heart, kidney, intestines, skeletal muscle, skin, or placenta; human yolk sac was not studied. 2) Radioactive transferrin was also present in rat yolk sac cultures, and the same protein was found in rat liver cultures as well. 3) Rat liver and rat placenta cultures both produced radioactive serum Ralpha(2)-globulin. Serum alpha-fetoprotein concentrations in the rat declined abruptly after birth to approximately half of the prenatal level by 2 to 3 days of age, in accord with the loss of the fetal membranes at delivery; the alpha-fetoprotein level then remained relatively constant until the rat was 6 to 8 days of age, after which synthesis of the protein was increasingly suppressed.

Animals↗