M/sub r/ 25,000 heparin-binding protein from guinea pig brain is a high molecular weight form of basic fibroblast growth factor

Journal Article · Sat Aug 01 00:00:00 EDT 1987 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.84.16.5778· OSTI ID:5172495

Moscatelli, D; Joseph-Silverstein, J; Manejias, R; Rifkin, D B

A M/sub r/ 25,000 form of basic fibroblast growth factor (bFGF) has been isolated from guinea pig grain along with the typical M/sub r/ 18,000 form. Both forms were purified to homogeneity by a combination of heparin-affinity chromatography and ion-exchange chromatography on an FPLC Mono S column. The M/sub r/ 25,000 form, like the M/sub r/ 18,000 form was not eluted from the heparin-affinity column with 0.95 M NaCl, but was eluted with 2 M NaCl. The M/sub r/ 25,000 guinea pig protein stimulated plasminogen activator production by cultured bovine capillary endothelial cells in a dose-dependent manner at concentration of 0.1-10 ngml, the same range that was effective for guinea pig and human M/sub r/ 18,000 bFGFs. The binding of human /sup 125/I-labeled bFGF to baby hamster kidney cells is inhibited equally by the M/sub r/ 25,000 guinea pig protein and the M/sub r/ 18,000 guinea pig and human bFGFs. Polyclonal antibodies raised against human bFGF recognize both the M/sub r/ 25,000 and 18,000 guinea pig proteins in an immunoblot analysis. In a radioimmunoassay, both the M/sub r/ 25,000 and M/sub r/ 18,000 guinea pig proteins compete equally well with iodinated human bFGF for binding to the anti-human bFGF antibodies. When treated with low concentrations of trypsin, the M/sub r/ 25,000 guinea pig bFGF was converted to a M/sub r/ 18,000 protein. These results show that the two molecules are closely related and suggest that the M/sub r/ 25,000 protein shares substantial homology with the M/sub r/ 18,000 bFGF

• Research Organization: New York Univ. Medical Center, NY (USA)
• OSTI ID: 5172495
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 84:16
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
CELL MEMBRANES
CONFIGURATION INTERACTION
GROWTH FACTORS
PURIFICATION
RADIOIMMUNOASSAY
BRAIN
DOSE-RESPONSE RELATIONSHIPS
FIBROBLASTS
GUINEA PIGS
HAMSTERS
IODINE 125
ION EXCHANGE CHROMATOGRAPHY
KIDNEYS
MOLECULAR WEIGHT
SOMATIC CELLS
ANIMAL CELLS
ANIMALS
BETA DECAY RADIOISOTOPES
BODY
CELL CONSTITUENTS
CENTRAL NERVOUS SYSTEM
CHROMATOGRAPHY
CONNECTIVE TISSUE CELLS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
IMMUNOASSAY
IMMUNOLOGY
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MAMMALS
MEMBRANES
MITOGENS
NERVOUS SYSTEM
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RADIOASSAY
RADIOIMMUNOLOGY
RADIOISOTOPES
RODENTS
SEPARATION PROCESSES
TRACER TECHNIQUES
VERTEBRATES
550601* - Medicine- Unsealed Radionuclides in Diagnostics