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S R Webb

Publications and source records attributed to S R Webb.

76 records · Page 5Linked to original sources

Mls determinants and anti-Mls receptors.

We review evidence from this laboratory that T cell recognition of Mlsa determinants is not controlled solely by the alpha-beta T cell receptor (TcR) molecule. We propose a model in which Mlsa recognition reflects a receptor-ligand interaction between two sets of complementary accessory molecules, one molecule (Mlsa) being expressed on B cells and the other (the anti-Mlsa receptor) on T cells; this interaction augments recognition of self class II molecules by the TcR. The biological role of Mls molecules might be to facilitate physiological T-B interaction.

Animals↗

Polyclonal-based ELISA for the identification of cyclohexanedione analogs that inhibit maize acetyl coenzyme-A carboxylase.

Cyclohexanedione herbicides inhibit monocotyledonous acetyl coenzyme-A carboxylase (ACCase; E.C. 6.4.1.2.), which catalyzes the first committed step in fatty acid biosynthesis. Although the target site has been identified, little is known about the mechanisms involved in herbicide binding. An immunological study was undertaken to create a model to better characterize the herbicide-enzyme interaction. Cyclohexanedione-specific antiserum was raised in New Zealand white rabbits by immunizing them with a cyclohexanedione analog-bovine serum albumin conjugate. Two indirect enzyme-linked immunosorbent assays (ELISA) were developed using 2 different cyclohexanedione analogs conjugated to ovalbumin as coating conjugates. Nineteen cyclohexanedione analogs, 13 active ACCase inhibitors, and 6 inactive analogs were tested for their ability to compete with both coating conjugates for antiserum binding. All active ACCase inhibitors were observed to compete with both coating conjugates, whereas all inactive analogs failed to compete with at least one coating conjugate. On the basis of these results, the immunological model could be used to distinguish all active ACCase inhibitors from inactive analogs using the 2 ELISAs sequentially.

Acetyl-CoA Carboxylase↗