Abstract:
A covalently reactive ligand analogue (CAL) of formula (1): wherein, L1 . . . Lx . . . Lm are components defining a ligand determinant, Lx is a component unit of the ligand determinant selected from the group consisting of an amino acid residue, sugar residue, a fatty acid residue and a nucleotide, L′ is a functional group of Lx, Y″ is atom, covalent bond or linker, Y′ is an optional charged or neutral group Y is a covalently reactive electrophilic group that reacts specifically with a receptor that binds to said ligand determinant, and n is an integer from 1 to 1000 m is an integer from 1 to 30.
Abstract:
Covalently reactive antigen analogs are disclosed herein. The antigens of the invention may be used to stimulate production of catalytic antibodies specific for predetermined antigens assocated with particular medical disorders. The antigen analogs may also be used to permanently inactivate endogenously produced catalytic antibodies produced in certain autoimmune diseases as well as in certain lymphoproliferative disorders.
Abstract:
Provided is a method for delivering a vasoactive intestinal polypeptide (VIP) liposome product to a target tissue of a mammal. The VIP is expressed on and in a liposome. Also provided is a method of preparing the VIP liposome product comprising cholesterol, phosphatidyl choline, and phosphatidyl glycerol.
Abstract:
Autoantibodies which enhance the rate of a chemical reaction of a substrate, processes for their preparation, their use and compositions thereof are disclosed. In particular, an autoantibody capable of catalyzing the hydrolysis of the peptide bond between amino acid residues 16 and 17 in the neurotransmitter vasoactive intestinal peptide (VIP) is disclosed. Human anti-thyroglobulin antibodies isolated by chromatography on protein-A and immobilized Tg hydrolyzed radiolabeled Tg, as shown by generation of several lower-sized products on SDS-electrophoresis gels. The activity displayed a K.sub.m value of a 39 nM property typical of an antibody-combining site. Tg-antibodies also hydrolyzed commercially available peptidyl-methylcoumarinamide (MCA) substrates, displaying a preference for arg-MCA and lys-MCA containing conjugates. The hydrolysis of pro-phe-arg-MCA was characterized by K.sub.m (17 .mu.M) and k.sub.cat 0.06 min.sup.-1. Peptidyl-MCA hydrolysis was inhibited potently by thyroglobulin (K.sub.i 24 nM), suggesting a catalytic site/located in the antibody combining site. In control experiments, the hydrolytic activities were removed by immunoadsorption with immobilized anti-human IgG, and IgG depleted of the Tg-specific antibodies by affinity chromatography did not display Tg and pro-phe-arg-MCA hydrolyzing activities.