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1.
Cutis ; 48(6): 457-8, 1991 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-1760936

RESUMO

Two cases of digitate dermatosis are presented. The clinical and histopathologic features of this unique entity are reviewed. We suspect that digitate dermatosis may be more prevalent than reported.


Assuntos
Dermatopatias/patologia , Humanos , Masculino , Pessoa de Meia-Idade
2.
J Biol Chem ; 257(8): 4564-9, 1982 Apr 25.
Artigo em Inglês | MEDLINE | ID: mdl-7068651

RESUMO

Bands 4.1 a and b are proteins of 80,000 and 78,000 molecular weight, which are both present at approximately 100,000 copies per erythrocyte ghost. Both proteins are components of the erythrocyte membrane skeleton. Bands 4.1 a and b are labeled when intact erythrocytes are incubated with [32P]orthophosphoric acid, and, therefore, are phosphoproteins. One-dimensional partial proteolytic mapping analysis of 32P-labeled bands 4.1 a and 4.1 b and two-dimensional peptide mapping analysis of 125I-labeled bands 4.1 a and 4.1 b clearly demonstrated that the two proteins are sequence-related phosphoproteins. Band 4.1 purified by standard techniques (Tyler, J. M., Hargreaves, W. R., and Branton, D. (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 5192-5196) contains bands 4.1 a and 4.1 b. Bands 4.1 a and 4.1 b bind to spectrin heterodimers in solution. We conclude that the erythrocyte skeletal proteins bands 4.1 a and 4.1 b are sequence-related phosphoproteins, both capable of binding spectrin.


Assuntos
Membrana Eritrocítica/análise , Eritrócitos/análise , Proteínas de Membrana/sangue , Fosfoproteínas/sangue , Eletroforese Descontínua , Humanos , Proteínas de Membrana/isolamento & purificação , Peso Molecular , Fragmentos de Peptídeos/análise , Fosfoproteínas/isolamento & purificação , Espectrina/isolamento & purificação
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