Leo T.O. Lee

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Glycophorin, the major sialoglycoprotein of the erythrocyte membrane, was extracted from human erythrocyte ghosts by the lithium diiodosalicylate phenol (LIS) or chloroform-methanol (CM) methods. The products (LISgp and CMgp) were examined for their capacity to inhibit invasion of erythrocytes by Plasmodium falciparum in vitro. In the presence of either(More)
An exponential gradient gel with 0-10% acrylamide and 0.5% agarose was developed for electrophoresis of intact high molecular weight lipoproteins. This system resolves very low density lipoproteins, intermediate density lipoproteins, lipoprotein a, and low density lipoproteins in a size-dependent fashion. The characteristic relative mobility of these(More)
Convalescent sera from proven cases of infection with Mycoplasma pneumoniae, and rabbit antisera to M. pneumoniae and to human erythrocyte glycoprotein contained cold hemagglutinins which were reactive only for human erythrocytes. Only the human serum cold agglutinins were inhibited by soluble integral glycoproteins derived from human erythrocyte ghosts by(More)
Lee, L. T. (Columbia University, New York, N.Y.), and C. Howe. Pneumoccal neuraminidase. J. Bacteriol. 91:1418-1426. 1966.-The elaboration of neuraminidase by pneumococci grown under optimal conditions in liquid medium was studied in relation to the bacterial growth cycle. The enzyme was found free in the culture medium in increasing concentration(More)
Amelotin (AMTN) is an ameloblast-secreted protein that belongs to the secretory calcium-binding phosphoprotein family, which also includes the enamel matrix proteins amelogenin, ameloblastin and enamelin. Although AMTN is supposed to play an important role in enamel formation, data were long limited to the rodents, in which it is expressed during the(More)
Heretofore, immunologic reagents used to define and quantify human Lp(a) have been polyclonal in origin and therefore heterogeneous in antigenic specificity. We report here the isolation of a mouse monoclonal antibody, LHLP-1, monospecific for Lp(a). The antigen reactive with LHLP-1 was expressed in both lipoprotein Lp(a) as well as apolipoprotein Lp(a)(More)