The authors give the schema of the different zones of the body and their points of measuring. They report on some average values registered with Szirmai's myotonometer on persons before and after massage. These myotonometric schemas play a new and important part in systematic measuring of muscles in the field of "Myologia practica".
en-copyright= kn-copyright= en-aut-name=SzirmaiEndre en-aut-sei=Szirmai en-aut-mei=Endre kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=JuranyiRobert en-aut-sei=Juranyi en-aut-mei=Robert kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= affil-num=1 en-affil= kn-affil=Aus dem Gerinnungsphysiologischen affil-num=2 en-affil= kn-affil=Praktischen Muskelunters Laboratorium END start-ver=1.4 cd-journal=joma no-vol=16 cd-vols= no-issue=2 article-no= start-page=99 end-page=111 dt-received= dt-revised= dt-accepted= dt-pub-year=1962 dt-pub=196204 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Enzymatic Studies of Glucuronide Formation in Impaired Liver III. Effects of Carbon Tetrachloride and Ectromelia Virus Infection on Liver Glucuronide Formation in Mouse en-subtitle= kn-subtitle= en-abstract= kn-abstract=Glucuronide formations by mouse liver homogenate in several liver impairments were studied by using 4-methyl umbelliferone as a glucuronide receptor. The results were as follows : 1. Subcutaneous or intraperitoneal administration of carbon tetrachloride to the mouse produced a significant increase in the liver glucuronyl transferase activity 12 or 24 hours after the treatment regardless of histological and enzymatic evidences of liver-cell necrosis. This increase was not attributed to the increase in the 'activator' of glucuronide formation but to the increase in the enzyme activity itself. 2. In Ectromelia virus mouse hepatitis, the glucuronyl transferase activity of the liver tissue was markedly reduced in severe cases. In moderate or milder cases, a slight increase in the activity was observed in a few of them in the early stage of the disease, and the activity was significantly decreased on the recovery in all of the cases which survived. 3. In the early stage of carbon tetrachloride injury when the glucuronyl transferase activity of whole mouse liver was increased and the decomposition of uridine diphosphate glucuronic acid by the liver tissue was also enhanced, the glucuronide formation in vivo was rather increased. It was thus considered that the whole liver glucuronyl transferase activity rather than the uridine diphosphate glucuronic acid content was responsible for the glucuronide formation in vivo as a rate-limiting factor.
en-copyright= kn-copyright= en-aut-name=TaketaKazuhisa en-aut-sei=Taketa en-aut-mei=Kazuhisa kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= affil-num=1 en-affil= kn-affil=Okayama University END start-ver=1.4 cd-journal=joma no-vol=16 cd-vols= no-issue=2 article-no= start-page=90 end-page=98 dt-received= dt-revised= dt-accepted= dt-pub-year=1962 dt-pub=196204 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Enzymatic studies of glucuronide formation in impaired liver. II. Activating effect of boiled liver extract on liver glucuronide formation en-subtitle= kn-subtitle= en-abstract= kn-abstract=The effect of the boiled liver extract on the velocity of 4-methyl umbelliferone lucuronide formation by mouse liver homogenate was studied. The results were as follows: 1. Addition of mouse or rat liver boiled extract to the complete system for the glucuronide formation produced an increase in the velocity of the glucuronide formation. 2. The boiled liver extract produced the increase in the velocity of the glucuronide formation not as a substrate but as an activator. 3, The activator in the boiled liver extract was relatively heat stable, acid labile, and precipitated as a fairly ethanol-soluble barium salt. The solution of the activator partially purified by ethanol fractionation of the barium salt indicated its absorption maximum at 262 mμ. These results suggested that the most possible substance in the boiled liver extract responsible for the activation of 4methyl umbelliferone glucuronide formation might be a sugar nucleotide.
en-copyright= kn-copyright= en-aut-name=TaketaKazuhisa en-aut-sei=Taketa en-aut-mei=Kazuhisa kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= affil-num=1 en-affil= kn-affil=Okayama University END start-ver=1.4 cd-journal=joma no-vol=16 cd-vols= no-issue=2 article-no= start-page=71 end-page=89 dt-received= dt-revised= dt-accepted= dt-pub-year=1962 dt-pub=196204 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Enzymatic Studies of Glucuronide Formation in Impaired Liver I. Assay Methods For the Determination of Glucuronyl Transferase Activity and Uridine Diphosphate Glucuronic Acid Content of Liver Tissue Using 4-Methyl Umbelliferone as a Glucuronide Receptor; Its Application to Needle Liver Biopsy Tissues en-subtitle= kn-subtitle= en-abstract= kn-abstract=An attempt was made to apply the method devised by ARIAS for the determination of liver glucuronyl transferase activity using 4-methyl umbelliferone as a glucuronide receptor to the small amounts of liver tissue obtained by needle biopsy. This was accomplished by studying the kinetics of enzymatic 4-methyl umbelliferone glucuronide formation by mean(of mouse liver homogenates. The improved method was proved to be applicable to human liver and gave a satisfactory result. In addition, an assay method for the estimation of liver uridine diphosphate glucuronic acid content from the amount of 4-methyl umbelliferone glucuronide formed from the uridine diphosphate glucuronic acid contained in the liver homogenate used as a source of glucuronyl transferase was studied, and as a result it was proved to be also applicable to the small amounts of human liver tissue.
en-copyright= kn-copyright= en-aut-name=TaketaKazuhisa en-aut-sei=Taketa en-aut-mei=Kazuhisa kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= affil-num=1 en-affil= kn-affil=Okayama University END