Purification, Characterization and Receptor Binding of Human Colony-Stimulating Factor-1 Page: 3
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units. Furthermore, the amino-terminal amino acid sequence
of the purified CSF-1 was elucidated as NH -Glu-Glu-Val-Ser-
Glu-Tyr-Cys-Ser-His-Met-Ile-Gly-Ser-Gly-His-Leu-Gln-Ser-Leu-
Gln-Arg-Leu-Ile. This partial amino acid sequence is
identical to the sequence of human urinary CSF and the
sequence derived from human CSF-1 cDNA.
The results from receptor binding studies suggested
that the human CSF-1 binding sites on mouse peritoneal
exudate macrophage (PEM) are the physiologically relevant
receptors as judged by the specificity, the high affinity
and the saturation. Equilibrium binding studies revealed
that there were approximately 80,000 binding sites/PEM with
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an apparent of 5.4 x 10 M. The binding activity of PEM
was inhibiteded by pretreatment with unlabeled CSF-1,
possibly due to the down regulation of receptors. The
recovery of binding activity is a temperature and protein
synthesis dependent process. In addition, the binding
activity was sensitive to trypsin treatment. Finally, the
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PEM-bound I-CSF-1 is degraded to smaller molecules at
37°C.
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Shieh, Jae-Hung. Purification, Characterization and Receptor Binding of Human Colony-Stimulating Factor-1, dissertation, May 1987; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc331991/m1/3/: accessed March 30, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .