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A basic somatomedin (SM) was purified from human plasma Cohn fraction IV-1 using an initial acid--ethanol--acetone extraction procedure followed by alternating molecular size or charge protein separation techniques. The final recovery of SM bioactivity was approximately 2% of that present in the starting Cohn fraction. The purified SM has an approximate molecular weight of 7500, pI 8.6, 4000 SM bioactivity units per milligram (as measured by a hypophysectomized rat bioassay) and a parallel approximately equipotent radioimmunoassay dose--response curve to SM-C and insulin-like growth factor-1 (IGF-I). Sodium dodecyl sulfate--polyacrylamide gel electrophoresis of this purified SM revealed a single protein band. The preliminary determination of the amino acid sequence of the N terminus suggested that this SM preparation was over 75% pure and the first five N-terminal amino acids were identical with those of IGF-I.
R M Bala, and
B Bhaumick
February 1986,
Acta endocrinologica,
R M Bala, and
B Bhaumick
January 1987,
Methods in enzymology,
R M Bala, and
B Bhaumick
January 1985,
Methods in enzymology,
R M Bala, and
B Bhaumick
May 1990,
Clinica chimica acta; international journal of clinical chemistry,
R M Bala, and
B Bhaumick
May 1978,
Biochimica et biophysica acta,
R M Bala, and
B Bhaumick
January 1988,
Endocrinology,
R M Bala, and
B Bhaumick
November 1990,
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R M Bala, and
B Bhaumick
June 1988,
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme,
R M Bala, and
B Bhaumick
August 2002,
Nihon rinsho. Japanese journal of clinical medicine,
R M Bala, and
B Bhaumick
January 1987,
International journal of radiation applications and instrumentation. Part B, Nuclear medicine and biology,
