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Literature DB >> 3325033

Immunochemical differentiation of glucose phosphate isomerase (GPI) allozymes of the mouse.

U Conrad¹, G Walter, D Helbing, R Manteuffel, J Schöneich.

Abstract

Polyclonal xenoantisera against mouse GPI-1B and GPI-1C were produced in rabbits and analyzed for their ability to recognize allozyme-specific determinants. These studies showed a high degree of serological similarity among the three allozymes of mouse glucose phosphate isomerase (GPI). However, GPI-1B and GPI-1C could be differentiated from GPI-1A as well as GPI-1A and GPI-1B from GPI-1C using quantitative solid-phase immunobinding assays. In addition, polyclonal and monoclonal alloantibodies specific for GPI-1C were produced in BALB/c (Gpi-1a/Gpi-1a) mice. As indicated by immunoblotting data, the allozyme specificity of rabbit antisera and monoclonal alloantibodies against GPI-1C is dependent on the native structure of that allozyme.

Entities: Gene Species

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Year: 1987 PMID： 3325033 DOI： 10.1007/bf00556216

Source DB: PubMed Journal: Biochem Genet ISSN： 0006-2928 Impact factor: 1.890

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References

27 in total

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Immunochemical differentiation of glucose phosphate isomerase (GPI) allozymes of the mouse.

1. Ovarian teratomas in mice are derived from oocytes that have completed the first meiotic division.

2. Antibodies to allozymes as potential cell markers for chimeric mouse studies.

3. Clonal origins of somites and their muscle derivatives: evidence from allophenic mice.

4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

5. Nitrocellulose membrane as an antigen or antibody carrier for screening hybridoma cultures.

6. Quantitative electrophoretic transfer of polypeptides from SDS polyacrylamide gels to nitrocellulose sheets: a method for their re-use in immunoautoradiographic detection of antigens.

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