Proceedings of the Japan Academy

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The vaginal epithelium of 'normal' ovariectomized adult mice of the C57 Black/MS strain was strongly mucified following 10 daily injections of 1mg progesterone. In vaginae showing estrogen-independent proliferation and cornification of the epithelium of 50% of ovariectomized adult mice given neonatal injections of 20μg estradiol-17β for 10 days, the cornification was not affected by 10 daily injections of 1mg progesterone, although it was totally inhibited or intermittently interrupted by progesterone injections in the rest of animals. The vaginal epithelium was seldom mucified. In estrogenized ovariectomized mice receiving two series of 10 daily injections of progesterone at an interval, vaginal smears were similar in type during the first and second injection periods. In contrast to this, vaginal response to the second series progesterone injections was different from that to the first in 35% of mice given vaginal instillations of 0.1% croton oil for 10 days following the first series injections. Cell populations of the epithelium may be qualitatively altered in inflamed vaginae of neonatally estrogenized mice.

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A three-day spleen culture technique for chromosome studies of mammals was described. The technique was advantageous for chromosome studies in aborted fetus and butchered animals as well as in small animals in which blood sampling is generally difficult.

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Crystallized trypsin inactivates M blood-group activity of human red blood cells and renders the treated red cells agglutinable with anti-N serum, and, on the other hand, releases a undialyzable M-active sialoglycopeptide from the red cells. The blood-group activity of N red cells against anti-N serum is hardly affected by the trypsin treatment, but a passable amount of a undialyzable N-active sialoglycopeptide is simultaneously liberated from the red cells.

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Three common phenotypes of the human hemoglobin-haptoglobin complexes were purified by ammonium sulfate fractionation, gel filtration on a Sephadex G-100 column, and chromatography nitrogen contents of the purified hemoglobin-haptoglobin complexes, it is suggested that each phenotype of haptoglobin molecule can combine with hemoglobin in the ratio of half a mol of hemoglobin to one mol of α and one mol of β haptoglobin chain.

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