TY - JOUR
T1 - Preparation and characterization of a sex-dependent rat urinary protein
AU - Roy, Arun K.
AU - Neuhaus, Otto W.
AU - Harmison, Charles R.
N1 - Funding Information:
This investigation was supported by grant AM 06705 of the U.S. Public Health Service.
PY - 1966/9/26
Y1 - 1966/9/26
N2 - 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.
AB - 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.
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U2 - 10.1016/0304-4165(66)90477-6
DO - 10.1016/0304-4165(66)90477-6
M3 - Article
C2 - 4165834
AN - SCOPUS:0014028888
SN - 0304-4165
VL - 127
SP - 72
EP - 81
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
IS - 1
ER -