Abstract: Ligands that bind to human selectin receptors are disclosed. The ligands are formulated with excipient carriers to form compositions which are administered to treated condition such as inflammation. The ligands have the structural formula III ##STR1## or molecules which have hydrogen bond donor groups equivalent to the circled groups with respect to their ability to form hydrogen bonds with a selectin under physiological conditions.

Abstract: Ligands in the form of N-acetyllactosamines which bind to endothelial leukocyte adhesion molecule-1 (ELAM-1) are disclosed. The ligand compounds can be formulated into pharmaceutical compositions and/or assay compositions used to alleviate inflammation and assay for the presence of (qualitative) and amount of (quantitative) ELAM-1 and thereby determine the presence, location and degree of inflammation.

Abstract: Ligands in the form of N-acetyllactosamines which bind to endothelial leukocyte adhesion molecule-1 (ELAM-1) are disclosed. The ligand compounds can be formulated into pharmaceutical compositions and/or assay compositions used to alleviate inflammation and assay for the presence of (qualitative) and amount of (quantitative) ELAM-1 and thereby determine the presence, location and degree of inflammation. The ligands are encompassed by general structural formula I as follows: ##STR1## wherein one of F and G is hydrogen and one is an N-acetyl neuraminic acid residue on the terminal unit and are both hydrogen on any other unit; J is hydrogen, a lactosylceramide or a linking group and K is hydrogen or a fucose residue and n is an integer of from 1 to 10 (preferably 3 or 4) with the proviso that n and K are defined such that at least one K is a fucose residue.

Abstract: Highly sulfated oligosaccharides in the form of hexasaccharide and octasaccharide compounds which have antiproliferative activity with respect to smooth muscle cells are useful in treatment of conditions characterized by unwanted smooth muscle cell proliferation such as a result of trauma or disease states such as asthma, congestive heart failure and hypertension. The oligosaccharides have increased ability to inhibit the proliferation of smooth muscle cells and decreased ability to act as an anticoagulant as compared with commercial heparin and/or unseparated fragments of heparin.

Abstract: Ligands in the form of N-acetyllactosamines which bind to endothelial leukocyte adhesion molecule-1 (ELAM-1) are disclosed. The ligand compounds can be formulated into pharmaceutical compositions and/or assay compositions used to alleviate inflammation and assay for the presence of (qualitative) and amount of (quantitative) ELAM-1 and thereby determine the presence, location and degree of inflammation. The ligands are encompassed by general structural formula I as follows: ##STR1## wherein one of F and G is hydrogen and one is an N-acetyl neuraminic acid residue on the terminal unit and are both hydrogen on any other unit; J is hydrogen, a lactosylceramide or a linking group and K is hydrogen or a fucose residue and n is an integer of from 1 to 10 (preferably 3 or 4) with the proviso that n and K are defined such that at least one K is a fucose residue.

Abstract: Ligands in the form of N-acetyllactosamines which bind to endothelial leukocyte adhesion molecule-1 (ELAM-1) are disclosed. The ligand compounds can be formulated into pharmaceutical compositions and/or assay compositions used to alleviate inflammation and assay for the presence of (qualitative) and amount of (quantitative) ELAM-1 and thereby determine the presence, location and degree of inflammation.

Abstract: Ligands in the form of N-acetyllactosamines which bind to endothelial leukocyte adhesion molecule-1 (ELAM-1) are disclosed. The ligand compounds can be formulated into pharmaceutical compositions and/or assay compositions used to alleviate inflammation and assay for the presence of (qualitative) and amount of (quantitative) ELAM-1 and thereby determine the presence, location and degree of inflammation. The ligands are encompassed by general structural formula I as follows: ##STR1## wherein one of A and B is hydrogen and one is an N-acetyl neuraminic acid residue; D and E are each independently hydrogen or a fucose residue; n is an integer of from 0 to 10 with the proviso that if n is 0, E is a fucose residue; F is hydrogen, a lactosylceramide residue or a linking group; and molecules equivalent to a compound of formula I regarding its ability to bind to an ELAM-1 receptor to the same degree as a compound of formula I.

Abstract: Saccharide in mixtures are separated into groups or individual saccharides and tested for their affinity for particular proteins. The method of the invention is carried out by conjugating saccharides in a mixture with charge-generating moieties and moieties capable of fluorescing such as 4-amino-1-naphthalene sulfonic acid (ANSA) to form conjugates. The saccharide conjugates are subjected to electrophoretic resolution within gels. The resolved bands of material can be seen under ultraviolet light and are electro-blotted onto charged nylon membranes to provide a stable record of the electrophoretic separation. The blots (visible under ultraviolet light) on the nylon membranes are brought into contact with particular proteins in order to determine the binding affinity of these particular proteins to particular saccharides on the nylon membrane. The proteins are preferably bound to labels so that the binding of the proteins to the saccharides can be easily detected.

Abstract: Separation methodology is disclosed which allows for the separation of mixtures of carbohydrates into highly resolved detectable bands of carbohydrates. The method involves first reacting a mixture of carbohydrates with charge generating moieties which are capable of fluorescing such as 1-amino-4-naphthalene sulfonic acid (ANSA) to form carbohydrate conjugates. The conjugates are subjected to a first-dimensional gel electrophoresis in a first direction to provide separate bands of carbohydrates in the gel. A band in the gel is removed and subjected to second-dimensional electrophoresis in a second direction which is substantially perpendicular to the first direction. More specific bands of more highly resolved carbohydrates are then formed in the second-dimensional gel. The more specific bands within the second-dimensional gel are then electro-blotted onto a substrate surface and can be viewed in extremely small amounts due to the fluorescent capability of the ANSA when viewed under ultraviolet light.

Abstract: A method of separating mixtures of saccharides into distinct detectable groups is disclosed. In accordance with the method a tri-functional conjugate must first be provided. The tri-functional conjugate is obtained by reacting a mixture of saccharides with moieties (a) capable of providing a charge upon ionization; (b) capable of fluorescing under ultraviolet light; and (c) having a light-activatable azido group thereon. The different functional moieties may all be present on the same moiety and connected directly to the saccharide or may be connected to each other wherein only one of the moieties is connected directly to the saccharide. The tri-functional conjugates are subjected to electrophoretic separation to obtain separate groups of conjugates in the gel. The groups of conjugates are transferred from the gel to the surface of a membrane which is exposed to light for a sufficient time and light frequency to activate the azido-group.

Abstract: A method of separating mixtures of saccharides into distinct detectable groups is disclosed. The method comprises modifying 1-amino-4-naphthalene sulfonic acid (ANSA) with a light-sensitive azido-group and binding the modified ANSA to saccharides to form ANSA/saccharide conjugates. The conjugates are subjected to electrophorectic separation to obtain separate groups of conjugates in the gel. The groups of conjugates are transferred from the gel to the surface of a membrane which is exposed to light for a sufficient time and light frequency to activate the azido-group. The light-activated azido-groups attached to the surface of the membrane. The ANSA/saccharides conjugates can then be contacted with labeled probes such as radiolabeled proteins to determine the affinity of the probes to particular saccharides.

Abstract: A glycosaminoglycoside (GAG) composition predominantly of tetrasacchardie units derived from heparin/heparan sulfate has enchanced activity in preventing the proliferation of smooth muscle cells. This GAG preparation is useful in the treatment of diseases characterized by unwanted smooth muscle cell proliferation and activity.

Abstract: Saccharide in mixtures are separated into groups or individual saccharides and tested for their affinity for particular proteins. The method of the invention is carried out by conjugating saccharides in a mixture with 4-amino-1-naphthalene sulfonic acid (ANSA) to form conjugates. The saccharide/ANSA conjugates are subjected to electrophoretic resolution within gels. The resolved bands of material are electro-blotted onto charged nylon membranes to provide a stable record of the electrophoretic separation. The blots on the nylon membranes are brought into contact with particular proteins in order to determine the binding affinity of these particular proteins to particular saccharides on the nylon membrane. The proteins are preferably bound to labels so that the binding of the proteins to the saccharides can be easily detected.

Abstract: Separation methodology is disclosed which allows for the separation of mixtures of carbohydrates into highly resolved detectable bands of carbohydrates. The method involves first reacting a mixture of carbohydrates with 1-amino-4-naphthalene sulfonic acid (ANSA) to form carbohydrate/ANSA conjugates. The conjugates are subjected to a first-dimensional gel electrophoresis in a first direction to provide separate bands of carbohydrates in the gel. A band in the gel is removed and subjected to second-dimensional electrophoresis in a second direction which is substantially perpendicular to the first direction. More specific bands of more highly resolved carbohydrates are then formed in the second-dimensional gel. The more specific bands within the second-dimensional gel are then electro-blotted onto a substrate surface and can be viewed in extermely small amounts due to the fluorescent capability of the ANSA when viewed under ultraviolet light.