-transparent.png){kind=logo}
A preparation of human pituitary somatotropin examined in quantitative polyacrylamide gel electrophoresis is conformationally compact. The derived molecular weight by quantitative electrophoresis is consistant with the known mass of the hormone and value obtained by other methods. A plasmin-modified somatotropin is more compact and shows full activity in immunoassay, and in lymphocyte binding and somatotropic assays, with enhanced lactogenic activity. The N-terminal 134-amino acid fragment and a hendekakaihekaton fragment exist in non-monomeric forms. The N-terminal fragment has immunologic and biologic activity, with greatest activity in the in vivo somatotropic assay. The hendekakaihekaton fragment exhibited only marginal activity. All preparations showed heterogeneity of charge in quantitative electrophoresis with discreet charge isomerism recognizable for the native and plasmin-modified preparations.
J S Skyler, and
A Chrambach, and
C H Li
January 1980,
Voprosy meditsinskoi khimii,
J S Skyler, and
A Chrambach, and
C H Li
October 1966,
Vnitrni lekarstvi,
J S Skyler, and
A Chrambach, and
C H Li
December 2020,
Cold Spring Harbor protocols,
J S Skyler, and
A Chrambach, and
C H Li
April 1971,
Science (New York, N.Y.),
J S Skyler, and
A Chrambach, and
C H Li
April 1973,
Zeitschrift fur klinische Chemie und klinische Biochemie,
J S Skyler, and
A Chrambach, and
C H Li
July 1975,
Biochimica et biophysica acta,
J S Skyler, and
A Chrambach, and
C H Li
January 1971,
Studii si cercetari de inframicrobiologie,
J S Skyler, and
A Chrambach, and
C H Li
June 1976,
The Journal of dairy research,
J S Skyler, and
A Chrambach, and
C H Li
January 1971,
Acta physiologica latino americana,
J S Skyler, and
A Chrambach, and
C H Li
April 1965,
Archives of biochemistry and biophysics,
