Structural modifications of acidic fibroblast growth factor alter activity, stability, and heparin dependence.
Thomas
K A
KA
Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065.
Ortega
S
S
Soderman
D
D
Schaeffer
M T
MT
DiSalvo
J
J
Gimenez-Gallego
G
G
Linemeyer
D
D
Kelly
L
L
Menke
J
J
D016475:3T3 Cells; D000595:Amino Acid Sequence; D000818:Animals; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D016220:Fibroblast Growth Factor 1 / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D066298:In Vitro Techniques; D051379:Mice; D008934:Mitogens; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011994:Recombinant Proteins; D016415:Sequence Alignment; D013329:Structure-Activity Relationship
D004220:Disulfides; D008934:Mitogens; D011994:Recombinant Proteins; D016220:Fibroblast Growth Factor 1; D003545:Cysteine