Abstract
The receptor on human neutrophils (polymorphonuclear leukocytes or PMN) that mediates cellular adherence has been purified from the peripheral blood PMN obtained from an individual with chronic myelogenous leukemia (CML). This receptor consists of two noncovalently associated subunits, designated αM (Mac-1α, CD11b) (M(r) = 170,000) and β (Mac-1β, CDw 18) (M(r) = 100,000) respectively, which are identical on normal and CML PMN. The subunits were purified by monoclonal antibody 60.1-Sepharose (anti-αM) affinity chromatography and separated in 5-nmol quantities by high pressure liquid chromatography on a TSK-4000 gel filtration column. Subunits were characterized by amino acid composition, NH2-terminal amino acid sequence, and carbohydrate content. The NH2-terminal sequence of the human PMN αM subunit contains regions of homology with the human platelet glycoprotein IIbα. We conclude that nanomole amounts of individual αM and β subunits of the receptor on human PMN that mediates cellular adherence can be isolated and separated using CML PMN.
| Original language | English |
|---|---|
| Pages (from-to) | 5576-5580 |
| Number of pages | 5 |
| Journal | Journal of Biological Chemistry |
| Volume | 262 |
| Issue number | 12 |
| State | Published - 1987 |
| Externally published | Yes |