Fujiki Y, Rathnam P, Saxena B B
Biochim Biophys Acta. 1980 Aug 21;624(2):428-35. doi: 10.1016/0005-2795(80)90084-7.
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.
用人促卵泡激素（FSH）与枯草杆菌蛋白酶、嗜热菌蛋白酶、溴化氰、链霉蛋白酶和胰蛋白酶进行消化，以分离含胱氨酸的肽段。这些肽段通过Sephadex G - 50柱凝胶过滤以及在pH 6、3.5和/或2条件下的高压纸电泳进行纯化。通过氨基酸组成、末端基团分析以及用埃德曼降解法测定氨基酸序列，确定了含胱氨酸肽段在人FSHα亚基和β亚基中的位置。结果表明，二硫键存在于人FSHα亚基中位于第7和10、28和87以及82和84位之间的半胱氨酸残基之间，以及β亚基中位于第3和28、17和51以及32和104位之间的半胱氨酸残基之间。
