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Precipitating, complement-fixing and neutralizing antibody was produced in rabbits by immunization with a partially purified human pituitary FSH preparation. Apparent serological specificity of this antiserum was increased after absorption with human serum and HCG. Attempts were made to examine immunologic carbohydrate determinant groups of human pituitary FSH by complement-fixation inhibition reactions between the absorbed antiserum and homogeneous human pituitary FSH preparations, using mono- and disaccharides, and by treatment of the hormone preparations with several carbohydrate-hydrolyzing enzymes. Of the saccharides tested, galactose, β-methyl- D-galactopyranoside lactose and melibiose were active in the inhibition test, and the disaccharides were more effective than the monosaccharides on an equimolar basis. Ovarian weight augmentation activity of FSH was completely abolished, but its complement-fixing property was not affected after treatment with neuraminidase. Both biologic and immunologic properties of FSH were resistant to either lysozyme or β-glucosidase. The complement-fixing property was hardly affected by combined treatment of FSH with neuraminidase and lysozyme but was reduced with increasing time of incubation with neuraminidase plus β-glucosidase. From these results it is tentatively concluded that neuraminic acid is essential for biologic activity but is not involved in the antigenic structure of human pituitary FSH and that a D-galactopyranosyl unit is a constituent of the antigenic determinant groups. (Endocrinology85:330,1969)
Kazutoshi Mori (Fri,) studied this question.