Glycogenolytic activities of partially purified fraction from dog pancreas following the administration of cobaltous chloride, synthalin A and alloxan were compared using the corresponding fraction from intact dogs as a standard.
Synthalin A treatment reduced and cobaltous chloride treatment increased the extractable glycogenolytic activity in dog pancreas.
The results are discussed in comparison with that of Fodden and Read (1954) in which rabbits were used as experimental animals.

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In a short period between the third and seventh day after section of the pituitary stalk, varying degree of regeneration of the portal vessels took place in the fibrous tissue around a waxed paper. Capillary network was too meager and slender to elicit a rapid and marked reactivity of the adenohypophysis in stress.
Injection of Pitressin caused increase in pituitary-adrenal function biologically and histologically in the stalk-cut dogs.In the same manner, Pitocin increased the pituitary gonadal function.
Surgical stressors, like burning and laparotomy, caused increase of pituitaryadrenaland-gonadal functions in the stalk-cut dogs in the same manner as in the dog with injection of Pitressin or Pitocin into the systemic circulation.
Brief discussion was made on the effect of stalk section and on the significance of the portal vessels on the anterior pituitary activity. It was suggested that the humoral stimulator could be transported into the anterior pituitary via the systemiccirculation.

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The activity of the pituitary growth hormone as a stimulant of the mitosis in tissues of the bull-frog tadpole and the adult newt was examined under the condition of thiourea treatment or in the absence of nervous influence in the limb. In the case of bull-frog tadpole, temporal mitosis-stimulating effect of the hormone took place with no bearing on the functional alteration of the thyroid which resulted by the concomitant thyrotropic hormone in this preparation. In some cases, the epidermal cells of the individuals which received the treatment of 0.05 per cent thiourea solution did not fully respond to the growth hormone as in the case of the normal individuals.
Transection of the third, fourth and fifth spinal nerves of the adult newt caused a tendency of decrease of the mitotic rate in the regenerating limb. When growth hormone was administered to such denervated animals, the epidermal cells of the denervated limb did not respond by significant increase of the mitotic rate, while in intact control side of the limb, mitotic increase resulted in considerable measure.

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With the male and female rats of Wistar strain, effects of the removal of some endocrine glands and of the corticoid replacement upon thyroidal uptake of I¹³¹ were investigated. The effects of adrenalectomy and of corticoid replacement upon the uptake varied depending on experimental conditions. After castration the uptake was significantly decreased in the male, whereas in the female it was singnificantly increased at 1 week but remained unchanged thereafter. It was significantly increased after thymectomy, and was unchanged after sialoadenectomy.

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Melanophore concentrating hormone (MCH) extractable from the pituitary as well as from the hypothalamus of the carp and the catfish was examined at its gross chemical properties with the following results:
1. MCH activity of extracts is largely impaired by trypsin, but remains unaffected in pepsin digestion.
2. MCH is soluble in acetone, but insoluble in ethanol, methanol, ethyl ether and chloroform.
3. In paper chromatography (butanol: acetic acid: water=4: 1: 5) MCH activity is found around the site of Rf. 0.13 and more significantly near Rf. 0.29.
4. Experiments with paper electrophoresis at pH8.6 and 4.9 showed that MCH moved for a short distance toward the cathode irrespective of pH.
5. In both paper chromatographic and paper electrophoretic analyses, MCH activity resided at the site, where no specific tinctorial response was detected with ninhydrine, BPB, potassium ferricyanide, PAS, Sudan III and Sudan Black.
6. MCH was not inactivated by choline esterase in human erythrocytes.
7. MCH was separable from MEH by adsorption to aluminum oxide, and eluted by stepwisely decreasing concentration of acetone. The melanophore concentrating activity was found in 100% and 80% acetone fractions, and in water fraction too. Polarographic study of these fractions showed that acetone fractions contained acetylcholine-like substance, and water fraction contained MCH which appeared different from acetylcholine.
8. Observed chemical properties of MCH were brought to comparison with those of other substances with similar melanophore activity or with related pharmacological and chemical properties.

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Activities of some potent synthetic adrenocorticoids and the original ones were compared by a new scoring method based upon the change in intravenous glucose tolerance curve in rat. 9α-FHC was the most potent, followed by Δ¹-9α-FHC, Δ¹-C, Δ¹-HC, HC and C, but without significant difference between the first and the second, and the fourth and the fifth of them.The method is expected to be useful for the estimation of glucocorticoid activity.

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A salivary gland hormone Parotin as well as horse serum albumin as a control substance have been labeled with radioactive iodine. The biological activity of the radioiodinated Parotin preparation has been largely retained. Characteristically large amount of radioactivity has been demonstrated in the liver and spleen at the 5th and 20th mins. after the administration of I¹³¹-labeled Parotin to rats. A gradual degradation of the labeled Parotin in vivo has been also observed.

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By the so-called dilution method, Parotin was found to decrease the rate of localization of radioactivity in the liver and spleen following the administration of I¹³¹-labeled Parotin to rats, and also to decrease the rate of degradation of the labeled Parotin in vivo. From these it was strongly suggested that Parotin as well as I¹³¹-labeled Parotin would localize characteristically in the liver and spleen, and that Parotin might be degraded in vivo in a similar manner as I¹³¹-labeled Parotin.

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