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Characterization of macrophage adhesion molecule

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00401a007· OSTI ID:5357864
Macrophage adhesion molecule (MAM), an abundant surface molecule which functions in the adhesion and spreading of guinea pig macrophages on surfaces, is characterized as a heterodimer of the trypsin- and plasmin-sensitive glycopeptide gp160 (MAM-..cap alpha..) and the glycopeptide gp93 (MAM-..beta..). The density of MAM molecules is estimated at 630,000 per macrophage on the basis of quantitative binding of /sup 125/I-labeled monoclonal antibody. The glycopeptide subunits display microheterogeneity on isoelectrofocusing; the pI is 5.8-6.3 for gp160 (MAM-..cap alpha..) and 6.4-7.0 for gp93 (MAM-..beta..). A neutrophil gp160, gp93 molecule was shown to be indistinguishable from macrophage MAM on the basis of electrophoresis, isoelectrofocusing, and reactivity with 10 monoclonal antibodies. A related heterodimer of gp93 associated with a larger, antigenically different glycopeptide (gp180, gp93)was identified on circulating lymphocytes. Cumulative properties indicate that MAM is the guinea pig analog of human Mo1 and mouse Mac-1.
Research Organization:
Center for Blood Research, Boston, MA
OSTI ID:
5357864
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 27:1; ISSN BICHA
Country of Publication:
United States
Language:
English

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