1988
DOI: 10.1016/s0021-9258(19)81379-0
|View full text |Cite
|
Sign up to set email alerts
|

Production, biological activity, and structure of recombinant basic fibroblast growth factor and an analog with cysteine replaced by serine.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

2
11
0

Year Published

1989
1989
2021
2021

Publication Types

Select...
9

Relationship

0
9

Authors

Journals

citations
Cited by 98 publications
(13 citation statements)
references
References 44 publications
2
11
0
Order By: Relevance
“…~NGF and EGF were prepared by the method of Mobley et al (1976) and Savage and Cohen (1972), respectively, bFGF used in all experiments was an analog with all haif-cystine residues replaced by serines (Fox et al, 1988) (kindly provided by Dr. Michael Fox, Amgen, Inc., Thousand Oaks, CA). PMA, 8-Br-cAMP, and sodium orthovanadate were from Sigma Chemical Co. (St. Louis, Mo.).…”
Section: Methodsmentioning
confidence: 99%
“…~NGF and EGF were prepared by the method of Mobley et al (1976) and Savage and Cohen (1972), respectively, bFGF used in all experiments was an analog with all haif-cystine residues replaced by serines (Fox et al, 1988) (kindly provided by Dr. Michael Fox, Amgen, Inc., Thousand Oaks, CA). PMA, 8-Br-cAMP, and sodium orthovanadate were from Sigma Chemical Co. (St. Louis, Mo.).…”
Section: Methodsmentioning
confidence: 99%
“…Two are conserved among all members of the FGF family (71) and may be important in determining the tertiary structure of bFGF through intramolecular disulfide bonds. The two remaining cysteines are not essential for biological activity (19). In recombinant bFGF produced in Escherichia cold, these two cysteines appear to remain reduced (19).…”
Section: Historymentioning
confidence: 99%
“…The two remaining cysteines are not essential for biological activity (19). In recombinant bFGF produced in Escherichia cold, these two cysteines appear to remain reduced (19). However, the two nonessential cysteines in natural bFGF may be involved in disulfide bonds with free cysteines since the initial amino acid analysis of bovine pituitary bFGF yielded six cysteines (14).…”
Section: Historymentioning
confidence: 99%
“…FGF2 is also called the basic fibroblast growth factor (bFGF). In 1974, it was first isolated from the bovine pituitary (Lemmon & Bradshaw, 1975), and in 1988, the first human recombinant FGF2 was reported (Fox et al, 1988). The molecular weight of its secreted isoform is 18 kDa.…”
Section: Discussionmentioning
confidence: 99%