Faculty Research 1980 - 1989


Normal content of brain spectrin-like protein in sph/sph mice.

Document Type


Publication Date



Autoradiography, Brain-Chemistry, Cerebellum: an, Electrophoresis-Polyacrylamide-Gel, Fluorescent-Antibody-Technic, Membrane-Proteins: an, Mice, Mice-Mutant-Strains, Nerve-Tissue-Proteins: an, Spectrin: an, Spherocytes: an, SUPPORT-NON-U-S-GOVT, SUPPORT-U-S-GOVT-P-H-S

First Page


Last Page


JAX Source

Br-J-Haematol. 1984 Oct; 58(2):277-88.


NS19357, HL26059, AM25305


In the erythrocytes of WBB6F1-sph/sph mice spectrin constitutes only approximately 1% of the total sph/sph membrane protein compared to approximately 23% in WBB6F1-+/+ controls. No increase in proteolytic degradation of spectrin in sph/sph erythrocyte membranes could be detected with antibodies directed against mouse erythrocyte spectrin or mouse brain spectrin-like protein. As attachment of normal spectrin to the erythrocyte membrane of these animals appeared to be normal, and as spectrin is not detected when whole sph/sph erythrocytes are solubilized in SDS for SDS PAGE, the deficient erythrocyte spectrin was probably due to diminished production. Brain spectrin-like protein, a nonerythroid spectrin analogue, is antigenically, morphologically and functionally related to erythrocyte spectrin, but appears by peptide mapping analysis to be a distinct gene product. It was found by protein- and antibody-staining of brain membranes to be present in normal concentrations in sph/sph animals. Indirect immunofluorescence of mouse brain tissue with anti-brain spectrin-like protein IgG or anti-erythrocyte spectrin IgG indicated that the distribution of brain spectrin-like protein was normal in sph/sph brain. Therefore the mutation causing diminished production of sph/sph erythrocyte spectrin does not affect the expression of this nonerythroid spectrin analogue.

Please contact the Joan Staats Library for information regarding this document.