Abstract: This invention relates to novel ?-galactosidases for the enzymatic removal of the immunodominant monosaccharides on blood products and tissues. Specifically this invention provides a novel family of ?3 glycosidases, used for the enzymatic removal of type B antigens from blood group B and AB reactive blood products, and the GaIiIi antigen from non-human animal tissues, thereby converting these to non-immunogenic cells and tissues suitable for transplantation.

Abstract: The present invention provides conjugates between Granulocyte Colony Stimulating Factor and PEG moieties. The conjugates are linked via an intact glycosyl linking group that is interposed between and covalently attached to the peptide and the modifying group. The conjugates are formed from both glycosylated and unglycosylated peptides by the action of a glycosyltransferase. The glycosyltransferase ligates a modified sugar moiety onto either an amino acid or glycosyl residue on the peptide. Also provided are pharmaceutical formulations including the conjugates. Methods for preparing the conjugates are also within the scope of the invention.

Abstract: The present invention provides polypeptides that include an O-linked glycosylation site that is not present in the wild-type peptide. The polypeptides of the invention include glycoconjugates in which a species such as a water-soluble polymer, a therapeutic agent of a biomolecule is covalently linked through an intact O-linked glycosyl residue to the polypeptide. Also provided are methods of making the peptides of the invention and methods, pharmaceutical compositions containing the peptides and methods of treating, ameliorating or preventing diseased in mammals by administering an amount of a peptide of the invention sufficient to achieve the desired response.

Abstract: The present invention provides modified platelets having a reduced platelet clearance and methods for reducing platelet clearance. Also provided are compositions for the preservation of platelets. The invention also provides methods for making a pharmaceutical composition containing the modified platelets and for administering the pharmaceutical composition to a mammal to mediate hemostasis.

Abstract: A novel gene defining a novel enzyme UDP-galactose: ?-D-galactose-R 4-?-D-galactosyltransferase, termed ?4Gal-T1, with unique enzymatic properties is disclosed. The invention provides isolated DNA molecules and DNA constructs encoding ?4Gal-T1 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting ?4Gal-T1 activity, as well as cloning and expression vectors including such DNA, host cells comprising DNA encoding ?4Gal-T1, and recombinant methods for providing ?4Gal-T1. The enzyme ?4Gal-T1 and ?4Gal-active derivatives thereof are disclosed. Further, the invention discloses methods of obtaining ?1, 4galactosyl glycosylated glycosphingolipids by use of an enzymatically active ?4Gal-T1 protein thereof or by using cells stably transfected with a vector including DNA encoding an enzymatically active ?4Gal-T1 protein as an expression system for recombinant production of such glycosphingolipids.

Abstract: The present invention provides modified platelets having a reduced platelet clearance and methods for reducing platelet clearance. Also provided are compositions for the preservation of platelets. The invention also provides methods for making a pharmaceutical composition containing the modified platelets and for administering the pharmaceutical composition to a mammal to mediate hemostasis.

Abstract: The present invention provides IFN-? conjugates including IFN-? peptides and modifying groups such as PEG moieties. The IFN-? peptide and modifying group are linked via an intact glycosyl linking group interposed between and covalently attached to the IFN-? peptide and the modifying group. The IFN-? conjugates are formed from glycosylated peptides by the action of a glycosyltransferase. The glycosyltransferase ligates a modified sugar onto an amino acid or a glycosyl residue on the IFN-? peptide. Also provided are methods for preparing the IFN-? conjugates, methods for treating various disease conditions with the IFN-? conjugates, and pharmaceutical formulations including the IFN-? conjugates.

Abstract: A novel gene defining a novel enzyme in the UDP-D-galactose: ?-N-acetylglucosamine / ?-N-acetylgalactosamine ?1,3galactosyltransferase family, termed ?3Gal-T5, with unique enzymatic properties is disclosed. The enzymatic activity of ?3Gal-T5 is shown to be distinct from that of previously identified enzymes of this gene family. The invention discloses isolated DNA molecules and DNA constructs encoding ?3Gal-T5 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting ?3Gal-T5 activity, as well as cloning and expression vectors including such DNA, cells transfected with the vectors, and recombinant methods for providing ?3Gal-T5. The enzyme ?3Gal-T5 and ?3Gal-T5-active derivatives thereof are disclosed, in particular soluble derivatives comprising the catalytically active domain of ?3Gal-T5.

Abstract: A novel gene defining a novel enzyme UDP-galactose: ?-D-galactose-R 4-?-D-galactosyltransferase, termed ?4Gal-T1, with unique enzymatic properties is disclosed. The invention provides isolated DNA molecules and DNA constructs encoding ?4Gal-T1 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting ?4Gal-T1 activity, as well as cloning and expression vectors including such DNA, host cells comprising DNA encoding ?4Gal-T1, and recombinant methods for providing ?4Gal-T1. The enzyme ?4Gal-T1 and ?4Gal-active derivatives thereof are disclosed. Further, the invention discloses methods of obtaining ?1, 4galactosyl glycosylated glycosphingolipids by use of an enzymatically active ?4Gal-T1 protein thereof or by using cells stably transfected with a vector including DNA encoding an enzymatically active ?4Gal-T1 protein as an expression system for recombinant production of such glycosphingolipids.

Abstract: The present invention provides polypeptides that include an O-linked glycosylation site that is not present in the wild-type peptide. The polypeptides of the invention include glycoconjugates in which a species such as a water-soluble polymer, a therapeutic agent of a biomolecule is covalently linked through an intact O-linked glycosyl residue to the polypeptide. Also provided are methods of making the peptides of the invention and methods, pharmaceutical compositions containing the peptides and methods of treating, ameliorating or preventing diseased in mammals by administering an amount of a peptide of the invention sufficient to achieve the desired response.

Abstract: The present invention features compositions and methods related to truncated mutants of ST6GalNAcI. In particular, the invention features truncated human, mouse, and chicken ST6GalNAcI polypeptides. The invention also features nucleic acids encoding such truncated polypeptides, as well as vectors, host cells, expression systems, and methods of expressing and using such polypeptides.

Abstract: The present invention provides modified platelets having a reduced platelet clearance and methods for reducing platelet clearance. Also provided are compositions for the preservation of platelets. The invention also provides methods for making a pharmaceutical composition containing the modified platelets and for administering the pharmaceutical composition to a mammal to mediate hemostasis.

Abstract: The present invention provides modified platelets having a reduced platelet clearance and methods for reducing platelet clearance. Also provided are compositions for the preservation of platelets. The invention also provides methods for making a pharmaceutical composition containing the modified platelets and for administering the pharmaceutical composition to a mammal to mediate hemostasis.

Abstract: A novel gene defining a novel human UDP-GlcNAc: Gal/Gl cNAc? 1-3GalNAc ??1, 6GlcNAc-transferase, termed C2/4GnT, with unique enzymatic properties is disclosed. The enzymatic activity of C2/4GnT is shown to be distinct from that of previously identified enzymes of this gene family. The invention discloses isolated DNA molecules and DNA constructs encoding C2/4GnT and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting C2/4GnT activity, as well as cloning and expression vectors including such DNA, cells transfected with the vectors, and recombinant methods for providing C2/4GnT. The enzyme C2/4GnT and C2/4GnT-active derivatives thereof are disclosed, in particular soluble derivatives comprising the catalytically active domain of C2/4GnT.

Abstract: A novel gene defining a novel enzyme in the UDP-D-galactose: b-N-acetyl-glucosamine ?-1,4-galactosyltransferase family, termed ?4Gal-T2, with unique enzymatic properties is disclosed. The enzymatic activity of ?4Gal-T2 is shown to be distinct from that of previously identified enzymes of this gene family. The invention discloses isolated DNA molecules and DNA constructs encoding ?4Gal-T2 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting ?4Gal-T2 activity, as well as cloning and expression vectors including such DNA, cells transfected with the vectors, and recombinant methods for providing ?4Gal-T2. The enzyme ?4Gal-T2 and ?4Gal-T2-active derivatives thereof are disclosed, in particular soluble derivatives comprising the catalytically active domain of ?4Gal-T2.

Abstract: The present invention relates to mutants of human growth hormone, which contain newly introduced N-linked or O-linked glycosylation site(s), such that these recombinantly produced polypeptides have glycosylation patterns distinctly different from that of the naturally occurring human growth hormone. The polynucleotide coding sequences for the mutants, expression cassettes comprising the coding sequences, cells expressing the mutants, and methods for producing the mutants are also disclosed. Further disclosed are pharmaceutical compositions comprising the mutants and method for using the mutants.

Abstract: Attachment of O-glycans to proteins is controlled by a large family of homologous polypeptide GalNAc-transferases. Polypeptide GalNAc-transferases contain a C-terminal sequence with similarity to lectins. This invention discloses that the putative lectin domains of GalNAc-transferase isoforms, GalNAc-T4, -T7, -T2, and -T3, are functional and recognize carbohydrates, glycopeptides, and peptides and discloses the lectin domains of GalNAc-T1-T16. These lectin domains have different binding specificities and modulate the functions of GalNAc-transferase isoforms differently. Novel methods for identification of inhibitors or modulators of binding activities mediated by lectin domains of polypeptide GalNAc-transferases are disclosed. Direct binding activity of GalNAc-transferase lectins has been demonstrated for the first time and methods to measure lectin mediated binding of isolated lectins or enzymes with lectin domains are disclosed.

Abstract: The present invention provides polypeptides that include an O-linked glycosylation site that is not present in the wild-type peptide. The polypeptides of the invention include glycoconjugates in which a species such as a water-soluble polymer, a therapeutic agent of a biomolecule is covalently linked through an intact O-linked glycosyl residue to the polypeptide. Also provided are methods of making the peptides of the invention and methods, pharmaceutical compositions containing the peptides and methods of treating, ameliorating or preventing diseased in mammals by administering an amount of a peptide of the invention sufficient to achieve the desired response.

Abstract: A novel gene defining a novel enzyme in the UDP-D-galactose: beta-N-acetylglucosamine/beta-N-acetylgalactosamine beta 1,3galactosyltransferase family, termed beta3Gal-T5, with unique enzymatic properties is disclosed. The enzymatic activity of beta3Gal-T5 is shown to be distinct from that of previously identified enzymes of this gene family. The invention discloses isolated DNA molecules and DNA constructs encoding beta3Gal-T5 and derivatives thereof by way of amino acid deletion, substitution or insertion exhibiting beta3Gal-T5 activity, as well as cloning and expression vectors including such DNA, cells transfected with the vectors, and recombinant methods for providing beta3Gal-T5. The enzyme beta3Gal-T5 and beta3Gal-T5-active derivatives thereof are disclosed, in particular soluble derivatives comprising the catalytically active domain of beta3Gal-T5.

Abstract: Novel methods for identification of inhibitors or modulators of binding activities mediated by lectin domains of polypeptide GalNAc-transferases are disclosed. Direct binding activity of GalNAc-transferase lectins has been demonstrated for the first time and methods to measure lectin mediated binding of isolated lectins or enzymes with lectin domains are disclosed. The present invention specifically discloses a novel selective inhibitor of polypeptide GalNAc-transferase lectin domains, which provides a major advancement in that this inhibitor and related inhibitors sharing common characteristics of activity bind lectin domains without serving as acceptor substrate for glycosyltransferases involved in synthesis of O-glycans. This inhibitor is represented by the O-anomeric configuration of GalNAc-benzyl, GalNAc?-benzyl.