Studies on the disulfide bonds in human pituitary follicle-stimulating hormone.
Human follicle-stimulating hormone (FSH) was digested with subtilisin, thermolysin, cyanogen gromide, pronase and trypsin to isolate the cystine-containing peptides. These peptides were purified by gel filtration through Sephadex G-50 column and by high-voltage paper electrophoresis at pH 6, 3.5 and/or 2. The location of the cystine-containing peptides in human FSH alpha- and beta-subunits was established by amino acid composition, end-group analysis and determination of the amino acid sequence by Edman degradation. The results indicate that the disulfide bonds are present between half-cystine residues located between positions 7 and 10, 28 and 87 and 82 and 84 in the alpha-subunit, and between positions 3 and 28, 17 and 51 and 32 and 104 in the beta-subunit of human FSH.
D000818:Animals; D002417:Cattle; D003488:Cyanogen Bromide; D003553:Cystine / Q000032:analysis; D004220:Disulfides / Q000032:analysis*; D005640:Follicle Stimulating Hormone; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D010902:Pituitary Gland / Q000032:analysis*; D011487:Protein Conformation; D012756:Sheep; D013045:Species Specificity; D013381:Subtilisins; D013552:Swine; D013820:Thermolysin
D004220:Disulfides; D010446:Peptide Fragments; D003553:Cystine; D005640:Follicle Stimulating Hormone; D013381:Subtilisins; D013820:Thermolysin; D003488:Cyanogen Bromide