Follistatin and method of purifying same

Details Follistatin and method of purifying same Follistatin and method of purifying same

C - Chemistry, Metallurgy

12

N

530/13, 195/1.23

C12N 15/16 (2006.01) C07H 21/04 (2006.01) C07K 14/435 (2006.01) C07K 14/47 (2006.01) C07K 14/575 (2006.01) C12N 15/09 (2006.01)

Patent

CA 1340972

Two follistatin proteins with inhibin-like activity were isolated from porcine follicular fluid using heparin-Sepharose affinity chromatography, followed by gel filtration on Sephacryl S-200 and then six steps of high-performance liquid chromatography. Each isolated molecule is a monomer having a molecular weight of at least about 32,000 daltons. Microsequencing revealed the NH2-terminal portions both to be Gly-Asn-Cys-Trp-Leu- Arg-Gln-Ala-Lys-Asn-Gly-Arg-Cys-Gln-Val-Leu. The larger protein has 315 residues and is believed to be glycosylated. The smaller protein is a 288-residue, C-terminally shortened version thereof. These proteins specifically inhibit basal secretion of FSH, but not of LH, in a rat anterior pituitary monolayer culture system. The half-maximal effective dose for both is 2.5-6.0 ng/ml. Human and rat follistatins exhibit very high homology with the porcine protein, with the human differing from porcine in only 4 residues out of 315 and with the rat differing from porcine in only 8 residues out of 315.

575768

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