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Purification of basic fibroblast growth factor and alkaline phosphatase from human placenta
Author(s) -
Costa MH,
Ho PL,
AM Silva,
Baptista GR,
Leite LC,
Crespo Cabrera J.,
Venturini KM,
Katz M.,
Liberman C.,
AR Silva
Publication year - 1993
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1993.tb00236.x
Subject(s) - placenta , concanavalin a , sepharose , placental alkaline phosphatase , alkaline phosphatase , biochemistry , chromatography , molecular mass , basic fibroblast growth factor , chemistry , affinity chromatography , biology , enzyme , growth factor , in vitro , pregnancy , fetus , genetics , receptor
Human placenta is an available hospital waste which is known to contain many valuable biochemicals that may be commercially exploited. Using placental tissue previously extracted for haemoderivatives, we purified basic fibroblast growth factor (bFGF), a soluble protein, and placental alkaline phosphatase (PALP), a membrane‐linked protein, as a coupled process. bFGF purification comprises three steps: extraction and chromatographies on S‐Sepharose and heparin‐Sepharose. The final product includes a major 17 kDa and a minor 16 kDa component with a specific activity of 8.0 times 10(6) units/mg yielding 0.5‐1.0 microgram/kg of placenta. PALP purification comprises four steps: acidic butan‐1‐ol extraction and chromatographies on Q‐Sepharose, concanavalin A‐Sepharose and Q‐Sepharose. The purified PALP has a molecular mass of 70 kDa, a specific activity of 800 units/mg and yielded 50 micrograms/kg of placenta. The results show the possibility of purifying substances in placental haemolysed blood, soluble products from placental cellular mass and proteins from the cellular membrane in a one‐stream process.