Chemical and Immunological Characterization of the Two a a-N-Acetylgalactosaminidases from Squid Liver (original) (raw)
SUBSTRATE SPECIFICITY AND INHIBITORY STUDIES OF α-N-ACETYLGALATOSAMINIDASE I AND II FROM STARFISH (Asterina amurensis
Md. Harun-or- Rashid
World J. Sci. Engineering, 2017
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Chemical and structural characterization of α-N-acetylgalactosaminidase I and II from starfish, asterina amurensis
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Alpha-N-acetylgalactosaminidase: Isolation, properties and distribution of the human enzyme
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Elizabeth Sutkowski
Biochemistry, 1990
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Purification and Characterization of -N-Acetylgalactosaminidases I and II from the Starfish Asterina amurensis
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2000
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Purification and Characterization of α-N-Acetylgalactosaminidases I and II from the StarfishAsterina amurensis
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Lysozyme bound to the D1.3 monoclonal antibody retains enzymatic activity in assays using N-acetylglucosamine oligomers as substrate
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Molecular Immunology, 1987
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Purification to homogeneity and enzymatic characterization of an alpha-N-acetylgalactosaminide alpha 2 leads to 6 sialyltransferase from porcine submaxillary glands
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The Journal of biological chemistry, 1979
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Purification to homogeneity of a β-galactoside α2→3 sialyltransferase and partial purification of an α-N-acetylgalactosaminide α2→6 sialyltransferase from porcine submaxillary glands
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Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6
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Purification to homogeneity and enzymatic characterisation of an α-N-acetyl-galactosamine α2 ± 6 sialotransferase from porcine submaxillary glands
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The Lectin Domain of UDP-GalNAc:Polypeptide N-Acetylgalactosaminyltransferase 1 Is Involved in O-Glycosylation of a Polypeptide with Multiple Acceptor Sites
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Substrate Specificities of Three Members of the Human UDP-N-Acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase Family, GalNAc-T1, -T2, and -T3
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