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Roses, Allen D

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BIOCHEMICAL STUDIES OF MEMBRANE PROTEINS IN DMD

Roses, Allen D

1 July 1977 - 30 June 1983
NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE
Total Funding: $ 605,401

FY 1982
5R01NS013455-06
$ 144,416
FY 1981
5R01NS013455-05
$ 135,165
FY 1980
2R01NS013455-04
$ 104,133
FY 1979
5R01NS013455-03
$ 73,246
FY 1978
5R01NS013455-02
$ 76,343
FY 1977
1R01NS013455-01
$ 72,098
 
 
$ 605,401
Abstract

This research proposes to define a unique biochemical abnormality in erythrocyte membrane spectrin that is characteristic of and specific to x-linked Duchenne muscular dystrophy. Using the abnormally increased (32P)-phosphorylation of erythrocyte protein band II as a marker, methods of peptide mapping and isolation are proposed that involve a number of peptide cleavage techniques. Methods of analysis include gel filtration, stacking polyacrylamide gel electrophoresis, and reverse phase high performance liquid chromatography. This proposal is the next phase of a long-term project to define the biochemical defect in Duchenne dystrophy, to determine the pathogenesis of the disease, and to use these data to develop diagnostic methods for patients, carriers, and fetuses at risk.

7 Resulting Publications

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