Pleasure, pain, and emotion

In this dissertation I analyse the concepts of pleasure and unpleasantness and outline an approach whereby the insights gained about pleasure and unpleasantness are applied to the analysis of a number of feeling and emotion concepts. In trying to understand what pleasure is and hew it is related to pain and unpleasantness, I tackle various basic questions about the role of pleasure, pain, and unpleasantness in motivation and about the intrinsic goodness of pleasure and the intrinsic badness of pain and unpleasantness. In pleasure's nature of being good, wanted, and sought and pairfs nature of being bad, unwanted, and avoided we locate the way in which pleasure and pain are opposites and the central defining properties of the 'pleasant' and the 'unpleasant'. Within my analysis of pleasure and unpleasantness I reach the conclusion that pleasure and unpleasantness are 'special experiences' : I explain what is involved in this claim and defend it against the objections which Ludwig Wittgenstein raised in his Private Language Argument. The view of the emotions which I outline and defend is the view which Aristotle, Spinoza, and many other philosophers have held. According to this view, emotions or 'feelings' such as con¬ fidence or fear, delight or misery, and pride or shame, are 'modes' of pleasure or unpleasantness. Given my views on pleasure and unpleasantness, it would follow that a number of emotions are, in part, the 'special experiences' of pleasure and unpleasantness

Site-Directed Mutagenesis Studies on the Lima Bean Lectin

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65875/1/j.1432-1033.1995.0958g.x.pd

INTERACTION OF CONCANAVALIN A WITH MODEL SUBSTRATES *

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/72701/1/j.1749-6632.1974.tb53040.x.pd

Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I-B 4 isolectin to αgalactosyl carbohydrate antigens in the surface phase

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/73881/1/j.1399-3089.2004.00108.x.pd

An Immunochemical Study of the Combining Sites of the Second Lectin Isolated from \u3ci\u3eBandeiraea simplicifolia\u3c/i\u3e (BS II)

Two lectins with different binding specificities have been isolated from extracts of seeds of Bandeiraea simplicifolia. The first, Bandeiraea lectin I [11] was specific for terminal non-reducing αDGalactosyl residues. It reacted with B substances from human ovarian cysts and with several galactomannans to form precipitin lines in agar gels. Polysaccharides with terminal αDGalactosyl residues, such as larch galactan, did not react. The lectin agglutinated B erythrocytes strongly but also reacted to a lower titre with A1 and very weakly with A2 erythrocytes [15, 28] indicating that terminal non-reducing αDGalNAc [24] can be accommodated in the-site to some extent. Recently, it was shown that B. simplicifolia lectin I (BS I) consists of five isolectins each of which is a tetrameric glycoprotein composed of A and B subunits; the A subunits are specific for αDGalNAc, the B subunits for αDGal [30]. The second lectin, Bandeiraea lectin II (BS II), isolated by affinity chromatography on chitin [13], is a glycoprotein (molecular weight 113,000) of four subunits of molecular weight 30,000. It does not agglutinate A, B or O erythrocytes. Quantitative precipitin assays showed it to react better with BSA conjugated to p-azophenyl αDGalNAc than with the β compound. In inhibition studies, the unusual observation was made that N,N’-diacetylchitobiose (DGlcNAcβ1 → 4DGlcNAc) and pNO2 phenyl αDGalNAc were highly active; methyl αDGalNAc was only one half as active but was eight times more active than methyl βDGlcNAc

Characterization of gangliosides from Ehrlich ascites tumour cells and their variants

Differences in the nature of the gangliosides present in two types of Ehrlich ascites tumour (EAT) cells, the adherent and non-adherent EAT cells, were studied. Gangliosides were isolated by DEAE Sephadex column chromatography and analysed by high-performance thin-layer chromatography (HPTLC). The non-adherent EAT (na-EAT) cells which grow in the peritoneal cavity of mice were selected for growth on basement membrane and tissue culture plastic to give the adherent EAT (a-EAT) cells. na-EAT cells contained 1.57 nmol lipid-bound sialic acid per mg protein and at least 12 different gangliosides, including major gangliosides such as GM3, GM2, GM1, GD3, GD1a and GT1b. On the other hand, the ganglioside pattern of a-EAT cells differed significantly from that of na-EAT cells, both quantitatively and qualitatively. The content of lipid-bound sialic acid in a-EAT cells was only 0.24 nmol per mg of protein. The gangliosides in a-EAT cells were characterized as GD1a and trisialogangliosides and, significantly, a-EAT cells did not contain monosialogangliosides. Neutral glycolipids were isolated from both cell lines and their patterns were compared. In contrast to the gangliosides pattern, their neutral glycolipid patterns were similar. Glucosylceramide and lactosylceramide were the major components in both types of cells. In addition to na- and a-EAT cells, a-EAT cells were passaged in mice by intraperitoneal injection, giving rise to a third variant (c/m EAT cells). We analysed the gangliosides in c/m EAT cells to determine whether there was a change in the ganglioside pattern found in na-EAT cells. After repeated passage of c/m EAT cells in mice, the pattern of gangliosides shifted to that of na-EAT cells. Alterations of ganglioside composition may be associated with the growth environment of the murine peritoneal cavity; alternatively, a selection process may have occurred.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/45681/1/10719_2004_Article_BF00731486.pd

Spatiotemporal expression patterns of sialoglycoconjugates during nephron morphogenesis and their regional and cell type-specific distribution in adult rat kidney

The expression of α2,6- and α2,3-linked sialic acids on N-glycans was studied in embryonic, postnatal, and adult rat kidney. Histochemistry and blotting using Polyporus squamosus and Sambucus nigra lectins for α2,6-linked sialic acids and the Maackia amurensis lectin for α2,3-linked sialic acids were performed and sialyltransferase activity was assayed. N-glycans with α2,6- and α2,3-linked sialic acid were differently expressed in the two embryonic anlagen and early stages of nephron. Metanephrogenic mesenchyme was positive for α2,3-linked sialic acid but not for the α2,6-linked one, which became detectable initially in the proximal part of S-shaped bodies. Collecting ducts were positive for α2,6-linked sialic acid, whereas α2,3-linked sialic acid was restricted to their ampullae. Although positive in embryonic kidney, S1 and S2 of proximal tubules became unreactive for α2,3-linked sialic acid in postnatal and adult kidneys. In adult kidney, intercalated but not principal cells of collecting ducts were reactive for α2,3-linked sialic acid. In contrast, α2,6-linked sialic acids were detected in all cells of adult kidney nephron. Blot analysis revealed a different but steady pattern of bands reactive for α2,6- and α2,3-linked sialic acid in embryonic, postnatal, and adult kidney. Activity of α2,6 and α2,3 sialyltransferases was highest in embryonic kidney and decreased over postnatal to adult kidney with the activity of α2,6 sialyltransferase always being three to fourfold that of α2,3 sialyltransferase. Thus, α2,6- and α2,3-linked sialic acids are differently expressed in embryonic anlagen and mesenchyme-derived early stages of nephron and show regional and cell type-specific differences in adult kidne

S1.23 Investigation of the sialyltransferases present in two populations of ehrlich ascites tumor cells

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/45635/1/10719_2005_Article_BF01209824.pd

Reexamination of the carbohydrate binding stoichiometry of lima bean lectin

The carbohydrate binding stoichiometry of lima bean lectin component III was reexamined using equilibrium dialysis and quantitative affinity chromatography following limited chemical modification. Equilibrium dialysis employing methyl[2-14C]benzamido-2-deoxy-[alpha]--galactopyranoside as ligand demonstrated that the lectin tetramer bound 4 mol of sugar with Kassoc = 1.44 +/- 0.13 x 103 m-1 (T = 5 [deg]C, pH 7.0, ionic strength 0.1). The previous report of two sites/tetramer [Bessler, W. and Goldstein, I. J. (1974) Arch. Biochem. Biophys. 165, 444] appears to be the result of partial inactivation of the lectin due to oxidation of essential thiol groups. Following limited chemical modification of the thiol groups by methyl methanethiosulfonate, multiple intermediate forms with reduced affinity for Synsorb A were obtained. The number and hemagglutinating activities of these intermediates provided further support for the presence of four carbohydrate binding sites on lima bean lectin component III.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/24856/1/0000283.pd