Preparation and characterization of a sex-dependent rat urinary protein

Arun K. Roy, Otto W. Neuhaus, Charles R. Harmison

Resultado de la investigación: Articlerevisión exhaustiva

79 Citas (Scopus)

Resumen

A major urinary protein of the male rat was purified by a combination of (NH4)2SO4 fractionation and chromatography on DEAE-cellulose. The molecular weight, sedimentation coefficient (s020,w) and isoelectric point were determined to be 26 400, 2.2.S and pH 3.4, respectively. Hexose, glucosamine and sialic acid were shown tobe 2%, 1.6% and 1.4%. The amino acid composition was also established. The electrophoretic migration was studied in starch-gel and immunoelectrophoretic systems. In the immunoelectrophoretic system, the purified protein migrated similarly to one of the major components of the total urinary proteins previously designated as a α2-globulin.

Idioma originalEnglish (US)
Páginas (desde-hasta)72-81
Número de páginas10
PublicaciónBBA - General Subjects
Volumen127
N.º1
DOI
EstadoPublished - sept 26 1966
Publicado de forma externa

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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