Summary. A single oral administration of centchroman (1·25 mg/kg) to adult female rats within 24 h of mating induced slight acceleration in the rate of transport of embryos through the oviducts. The compound did not seem to produce any deleterious effect on preimplantation embryonic development since well organized and apparently normal embryos were collected from the genital tract up to Day 12 of pregnancy. The recovery rate of embryos from centchroman-treated rats was, however, significantly reduced after Day 4 of pregnancy. There was some stimulation in the rate of cleavage of embryos and morula to blastocyst transformation, but retardation in the shedding of the zona pellucida. The rate of blastocyst formation was not altered when 6–8-cell embryos collected from the oviducts of control rats were transferred to the uteri of control or centchroman-treated females. A delay in zona shedding was observed in the centchroman-treated recipients.
M. M. Singh, V. Bhalla, V. Wadhwa, and V. P. Kamboj
V. K. BHALLA, W. L. TILLMAN, and W. L. WILLIAMS
The concept of sperm acrosomes as modified lysosomes which evolved to facilitate fertilization in multicellular organisms has recently been proposed (Allison & Hartree, 1968, 1970). The following lysosomal enzymes have been found in sperm acrosomes: hyaluronidase and neuraminidase (Hartree & Srivastava, 1965; Srivastava, Adams & Hartree, 1965; Srivastava, Zaneveld & Williams, 1970), β-N-acetyl glucosaminidase (Conchie & Mann, 1957), acid phosphatase, phospholipase A and aryl sulphatase (Allison & Hartree, 1970), aryl amidase (Meizel & Colham, 1972) and acrosomal proteinases (Stambaugh & Buckley, 1968, 1969; Zaneveld, Srivastava & Williams, 1969; Zaneveld, Polakoski & Williams, 1972; Polakoski, Zaneveld & Williams, 1972). This paper concerns a lysosomal enzyme which cleaves the linkage between aspartate and N-acetyl glucosamine using the synthetic substrate, 2-acetamido-l-(l-aspartamido) 1,2 dideoxy glucose (Cyclo Chemical Corp., Box 71557, Los Angeles, Calif.). The enzyme, β-aspartyl