Abstract
The three ectoenzyme activities, NAD+ glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase were purified to homogeneity from solubilized human erythrocyte membranes. The purification procedure involved three sequential chromatography steps on hydroxylapatite, immobilized Cu++ and immobilized anti-CD38 monoclonal antibody resins. The final step yielded a single 46 kDa protein displaying all three enzymatic activities. Since the protein bound specifically to the anti-CD38 resin, it was immunologically identified as CD38, a 46 kDa surface antigen involved in activation and proliferation of lymphocyte populations.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ADP-ribosyl Cyclase
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ADP-ribosyl Cyclase 1
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Antigens, CD / blood*
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Antigens, CD / isolation & purification
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Antigens, Differentiation / blood*
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Antigens, Differentiation / isolation & purification
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Chlorides / pharmacology
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Chromatography
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Copper / pharmacology
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Durapatite
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Electrophoresis, Polyacrylamide Gel
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Erythrocyte Membrane / enzymology*
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Humans
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Kinetics
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Membrane Glycoproteins
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Molecular Weight
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N-Glycosyl Hydrolases / blood*
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N-Glycosyl Hydrolases / isolation & purification
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NAD+ Nucleosidase / blood*
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NAD+ Nucleosidase / isolation & purification
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Zinc Compounds / pharmacology
Substances
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Antigens, CD
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Antigens, Differentiation
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Chlorides
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Membrane Glycoproteins
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Zinc Compounds
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Copper
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zinc chloride
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Durapatite
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N-Glycosyl Hydrolases
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ADP-ribosyl Cyclase
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CD38 protein, human
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NAD+ Nucleosidase
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ADP-ribosyl Cyclase 1
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cupric chloride