Immunoreactivity of the two common allozymes of murine glucosephosphate isomerase

✍ Scribed by John Gearhart; Mary Lou Oster-Granite; James M. Musser

• Book ID: 104784122
• Publisher: Springer
• Year: 1981
• Tongue: English
• Weight: 526 KB
• Volume: 19
• Category: Article
• ISSN: 0006-2928
• DOI: 10.1007/bf00484617

✦ Synopsis

There are two common electrophoretic variants (allozymes) of murine glucosephosphate isomerase (GPI). In order to develop immunocytochemical procedures that are aIlozyme-specific, the two variants (GPI-1A and GPI-1B) were purified from skeletal muscle of several mouse strains and used as antigens for the elicitation of antibodies. The allozymes were purified to a specific activity of 800 units/mg by substrate elution from cellulose phosphate. When the purified allozymes were presented as antigens to goats, rabbits, and mice (both syngeneically and allogeneically), the goats and rabbits produced high titers of anti-GP1 antibody, but no humoral antibody was detected in the mice, as determined by radioimmunoassays. Antisera specific for the GPI-1B variant were enriched by absorbing selected sera with GPI-1A conjugated to Sepharose 4B. No antisera specific for GPI-IA were detected following the immunizations. The specificity of the anti-GPI-1B antisera provides a unique opportunity for the development of immunocytochemical procedures for studying the distribution of this allozyme in chimeric mouse tissues.