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Volume 272, Number 20, Issue of May 16, 1997 pp. 13117-13125
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification of the CD45-associated 116-kDa and 80-kDa Proteins as the alpha - and beta -Subunits of alpha -Glucosidase II

(Received for publication, February 13, 1997, and in revised form, March 17, 1997)

Christopher W. Arendt and Hanne L. Ostergaard

From the Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

CD45 is an abundant, highly glycosylated transmembrane protein-tyrosine phosphatase expressed on hematopoietic cells. Herein we demonstrate that two proteins of 116 kDa and 80 kDa copurify with CD45 from mouse T cells. Microsequence analysis of the 116-kDa protein revealed high similarity to an incomplete human open reading frame that has been suggested to correspond to the catalytic alpha -subunit of glucosidase II. We determined the nucleotide sequence of the mouse cDNA and observed that it encodes a protein product nearly identical to its human homologue and shares an active site consensus sequence with Family 31 glucosidases. Amino acid sequencing of the 80-kDa protein, followed by molecular cloning, revealed high homology to human and bovine cDNAs postulated to encode the beta -subunit of glucosidase II. Antisera developed to the mouse beta -subunit allowed us to demonstrate that the interaction between CD45 and glucosidase II can be reconstituted in vitro in an endoglycosidase H-sensitive manner. The strong interaction between glucosidase II and CD45 may provide a paradigm for investigating novel aspects of the biology of these proteins.


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