Abstract
Fibroblast growth factor (FGF) from bovine brain has been reported to be a family of three polypeptide fragments derived by limited proteolysis from myelin basic protein (MBP) (Westall, F.C., Lennon, V.A., and Gospodarowicz, D. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 4675-4678). However, fragments of sequence similar to the proposed active ones, generated from bovine MBP) by acid proteases, are inactive in stimulating [ 3H]thymidine incorporation in BALB/c 3T3 cells. Further, the principal active component of the brain FGF preparation (Gospodarowicz, D., Bialecki, H., and Greenburg, G. (1978) J. Biol. Chem. 253, 3736-3743) which can be recovered in high yield from isoelectric focusing in sucrose has a pI between 4.8 and 5.8 in contradistinction to the MBP fragments (pI ~ 10) and is not retained on a column of chicken anti-bovine MBP-Sepharose. Therefore, although the reported preparation of brain FGF gives an increase in activity units/mg of protein of about 1000-fold over the crude brain extract, the main protein components, the MBP fragments, do not possess the mitogenic activity. Additional purification of as much as 50- to 100-fold may be required to obtain a homogeneous preparation of the real brain FGF.
| Original language | English |
|---|---|
| Pages (from-to) | 5517-5520 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 255 |
| Issue number | 12 |
| State | Published - Dec 1 1980 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Brain fibroblast growth factor. Nonidentity with myelin basic protein fragments. / Thomas, K. A.; Riley, M. C.; Lemmon, Sandra; Baglan, N. C.; Bradshaw, R. A.
In: Journal of Biological Chemistry, Vol. 255, No. 12, 01.12.1980, p. 5517-5520.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Brain fibroblast growth factor. Nonidentity with myelin basic protein fragments
AU - Thomas, K. A.
AU - Riley, M. C.
AU - Lemmon, Sandra
AU - Baglan, N. C.
AU - Bradshaw, R. A.
PY - 1980/12/1
Y1 - 1980/12/1
N2 - Fibroblast growth factor (FGF) from bovine brain has been reported to be a family of three polypeptide fragments derived by limited proteolysis from myelin basic protein (MBP) (Westall, F.C., Lennon, V.A., and Gospodarowicz, D. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 4675-4678). However, fragments of sequence similar to the proposed active ones, generated from bovine MBP) by acid proteases, are inactive in stimulating [ 3H]thymidine incorporation in BALB/c 3T3 cells. Further, the principal active component of the brain FGF preparation (Gospodarowicz, D., Bialecki, H., and Greenburg, G. (1978) J. Biol. Chem. 253, 3736-3743) which can be recovered in high yield from isoelectric focusing in sucrose has a pI between 4.8 and 5.8 in contradistinction to the MBP fragments (pI ~ 10) and is not retained on a column of chicken anti-bovine MBP-Sepharose. Therefore, although the reported preparation of brain FGF gives an increase in activity units/mg of protein of about 1000-fold over the crude brain extract, the main protein components, the MBP fragments, do not possess the mitogenic activity. Additional purification of as much as 50- to 100-fold may be required to obtain a homogeneous preparation of the real brain FGF.
AB - Fibroblast growth factor (FGF) from bovine brain has been reported to be a family of three polypeptide fragments derived by limited proteolysis from myelin basic protein (MBP) (Westall, F.C., Lennon, V.A., and Gospodarowicz, D. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 4675-4678). However, fragments of sequence similar to the proposed active ones, generated from bovine MBP) by acid proteases, are inactive in stimulating [ 3H]thymidine incorporation in BALB/c 3T3 cells. Further, the principal active component of the brain FGF preparation (Gospodarowicz, D., Bialecki, H., and Greenburg, G. (1978) J. Biol. Chem. 253, 3736-3743) which can be recovered in high yield from isoelectric focusing in sucrose has a pI between 4.8 and 5.8 in contradistinction to the MBP fragments (pI ~ 10) and is not retained on a column of chicken anti-bovine MBP-Sepharose. Therefore, although the reported preparation of brain FGF gives an increase in activity units/mg of protein of about 1000-fold over the crude brain extract, the main protein components, the MBP fragments, do not possess the mitogenic activity. Additional purification of as much as 50- to 100-fold may be required to obtain a homogeneous preparation of the real brain FGF.
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UR - http://www.scopus.com/inward/citedby.url?scp=0019308952&partnerID=8YFLogxK
M3 - Article
C2 - 6445901
AN - SCOPUS:0019308952
VL - 255
SP - 5517
EP - 5520
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 12
ER -