Opsonic properties of human serum alpha-2 hs glycoprotein
CJ Van Oss, CF Gillman, PM Bronson… - Immunological …, 1974 - Taylor & Francis
CJ Van Oss, CF Gillman, PM Bronson, JR Border
Immunological communications, 1974•Taylor & FrancisHuman serum α2HS glycoprotein (α2HS) has been isolated to a purity of more than 95%. At
a concentration of 0.1%= α2HS significantly enhances the phagocytosis of Escherichia coli
and of Staphylococcus aureus by human neutrophils in vitro. At the same concentration,
α2HS causes an increase in the hydrophobicity of these microorganisms, as measured by
the sessile saline drop contact angle method. The level of α2HS is much decreased in the
sera of trauma patients. Alpha-2 HS may be the human homologue of the recently described …
a concentration of 0.1%= α2HS significantly enhances the phagocytosis of Escherichia coli
and of Staphylococcus aureus by human neutrophils in vitro. At the same concentration,
α2HS causes an increase in the hydrophobicity of these microorganisms, as measured by
the sessile saline drop contact angle method. The level of α2HS is much decreased in the
sera of trauma patients. Alpha-2 HS may be the human homologue of the recently described …
Human serum α2HS glycoprotein (α2HS) has been isolated to a purity of more than 95%. At a concentration of 0.1%= α2HS significantly enhances the phagocytosis of Escherichia coli and of Staphylococcus aureus by human neutrophils in vitro. At the same concentration, α2HS causes an increase in the hydrophobicity of these microorganisms, as measured by the sessile saline drop contact angle method. The level of α2HS is much decreased in the sera of trauma patients. Alpha-2 HS may be the human homologue of the recently described rat α2 opsonic protein (1).
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