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Volume 43, Issue 1
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Tsutomu YOSHIDA1972 Volume 43 Issue 1 Pages 1-10
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
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VI. Genetic control of serum cholinesterase isozyme, C3 zone, in miceMasaharu MANDA, Yoshio OKI, Shusaku NISHIDA1972 Volume 43 Issue 1 Pages 11-15
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESSThe sera of the CFW, dd, KK and DSD strain and some of their crossbreds were examined for inheritance in serum cholinesterase isozyme, C3 zone, which was detected by starch-gel electrophoresis combined with histochemical staining method. Some castrated mice and immature mice (21 days) in the CFW, NC and DSD strain were used to examine whether differences of the activity-levels of C3 zone among strains may be due to differences in the sex hormone.
The results were summarized as follows:
1) The activity-level of C3 zone in the castrated mice and immature mice of both sexes from the CFW, NC and DSD strain showed differences among strains as well as in the normal adult mice. The results suggested that differences among strains of activity-levels of C3 zone were independent to the sex hormone.
2) From mating result, the activity-levels of C3 zone from F1 progeny of crosses between the dd strain and the DSD strain showed intermediate activities between both parents. In the expected ratio, 1:2:1, the three phenotypes, high, intermediate and low active patterns, were obtained in F2 progeny. Crosses between the CFW strain and the KK strain conducted gave the same result.
In consequence of number of cross-tests, it was suggested that the three esterase phenotypes in mice were genetically controlled by a pair of autosomal codominant alleles designated as ChE and Che. Thus we conclude that the activity-levels of serum cholinesterase isozyme, C3 zone, in mice may be controlled not only genetically but also physiologically by sex hormone.View full abstractDownload PDF (1301K) -
VII. Genetic control of serum aliesterase isozyme, A4 zone in miceMasaharu MANDA, Yoshio OKI, Shusaku NISHIDA1972 Volume 43 Issue 1 Pages 16-19
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESSThe sera of 4 mouse strains, namely the C3H/He, CFW, KK and DSD strain, and some of their crossbreds were examined for inheritance in serum aliesterase isozyme, A4 zone which was detected by starch-gel electrophoresis combined with histochemical staining method. Some castrated mice in the CFW, NC and DSD strain were used to examine whether differences of the activity-levels of A4 zone among strains may be due to differences in sex hormone.
The results were summarized as follows;
1) The activity-levels of A4 zone in the castrated mice of both sexes from the CFW, NC and DSD strain showed differences among strains as well as in normal adult mice. The results suggested that differences of activity-levels of A4 zone among strains were independent to sex hormone.
2) From mating result, the activity-levels of A4 zone from F1 progeny of crosses between the C3H/He strain and the DSD strain showed intermediate (low) activities between both parents. In the expected ratio, 1:2:1, the three phenotypes, high, low and negative patterns, were obtained in F2 progeny. Crosses between the CFW strain and the KK strain conducted gave the same result.
3) In consequence of a number of cross-tests, it was suggested that the three esterase phenotypes in mice were genetically controlled by a pair of autosomal codominant alleles designated as AliE and Alie.View full abstractDownload PDF (678K) -
II. Hydrolysis and hydrogenation of lipids in an artificial rumenKeiichi TANAKA, Hideo HAYASHI1972 Volume 43 Issue 1 Pages 20-25
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESS1) Safflower oil, linoleic acid, linseed oil or linolenic acid was incubated with the rumen liquor in an artificial rumen and samples of the reaction medium were taken from the apparatus after various time intervals.
2) When safflower or linseed oil was incubated with the rumen liquor, hydrolysis of triglycerides occurred very rapidly in the reaction medium and the concentration of unesterified fatty acids increased correspondingly.
3) 18: 2 or 18: 3 derived from safflower or linseed oil was rapidly hydrogenated to 18:0.
4) When linoleic acid was incubated with the rumen liquor, little or no 18:0 was produced and 18: 1 markedly accumulated.
5) When linolenic acid was incubated with the rumen liquor, 18: 2 accumulated until 5 hours of the incubation. 18: 1 began to increase after 3 hours until the end of the experiment.View full abstractDownload PDF (368K) -
Keisuke KATOH1972 Volume 43 Issue 1 Pages 26-30
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESSThe author reported in a previous paper that there seemed to exist a "critical value" in dietary copper level (nearly 24μg in daily ration of 15g or 1.6ppm) above which the daily urinary copper excretion of adult male rat was almost constant regardless of the amount of copper ingested.
The present experiments were conducted to observe if the decrease in urinary copper excretion of the rats on low-copper diet was related to any change in blood copper level.
Exp. I: Each two of the ten adult female rats of Wistar strain were supplied with the diet containing 0.576, 1.08, 1.58, 2.58 and 4.58ppm copper. The basal diet contained 0.576ppm copper, and the additional copper was supplied as copper chloride. Urine samples were collected using a glassplate-type urine-feces separator. At the end of the experiment, the rats were killed and blood and liver samples were obtained.
The rats that ingested the smallest amount (0.576ppm) of copper excreted less copper (0.3 and 0.7μg/head•day) in the urine than any other rats during 25th through 30th day. However, among the rats fed with the diet containing 1.08-4.58ppm copper, there was no difference in urinary copper excretion (1.3±0.2(S. D.)μg/head•day). It indicates that the"critical value" in adult female rat exists between 0.6 and 1.1ppm. Serum copper levels paralleled the amounts of copper excreted in the urine. With the increase of copper in the diet the liver copper levels increased from 12 to 24ppm (dry base).
Exp. II: Seven-month-old male rats of Wistar strain were treated with two dietary levels of copper (0.628 or 14.0ppm) and water (20 or 40ml/head•day). Two rats were subjected to each treatment.
The rats on low-copper diet excreted less copper in urine (1.3±0.2μg/head•day) than those on high-copper diet (3.5±0.3μg/head•day) during 25th through 30th day. It can be explained by an assumption that 0.628ppm was below the "critical level" of dietary copper for the adult male rat (nearly 1.6ppm). Serum copper level was also lower in the rats fed low-copper diet. Difference in the amount of water intake had no effect on the urinary excretion of copper. This means that it is unnecessary to consider water consumption or urine volume in discussing urinary copper excretion, so long as water consumption is within normal range. Difference in dietary copper levels, although greater than in Exp. I, did not cause much difference in liver copper levels.
Blood copper level has been reported to be usually constant according to the species, sex or age, when the animal ingests enough copper. In the above two experiments, blood copper level almost paralleled urinary copper excretion and seemed to directly influence the urinary copper level when blood copper level decreases as a result of less copper intake. It seems possible from urinary copper level to assume the copper status of the animal, and also to mention the factors which influence copper utilization.View full abstractDownload PDF (372K) -
Yasuo IGARASHI, Zenichi SAITO1972 Volume 43 Issue 1 Pages 31-38
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESSTS-casein was separated from temperature sensitive fraction by adsorption on TEAE cellulose at 40°C and recovered by cooling the adsorbent to 2-4°C in the same buffer solution. TS-casein separated by this procedure agreed with that previously described in respect to gel filtration on Sephadex G-100, and consisted of a major and two minor components by starch gel electrophoresis in the presence of 7M urea and 0.022M 2-mercaptoethanol. An electro-focusing experiment showed two major components (isoelectric point: 6.7 and 7.3) in the existence of 5M urea.
Each addition of 5% (at the final concentration) methanol, ethanol, n-propanol, and n-buthanol to TS-casein solution affected its turbidity curve. In a 25% ethanol solution, TS-casein precipitated in a wide pH range (4.1-8.8). The minimum stability in 50% ethanol was observed at pH 5.9-6.9 and the stability was higher than in 25% ethanol except in this pH range.View full abstractDownload PDF (662K) -
I. Production and some properties of the extracellular proteaseFumisaburo TOKITA, Akiyoshi HOSONO1972 Volume 43 Issue 1 Pages 39-48
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESSIn the present study the production of extracellular protease by Brevibacterium linens and some properties of the extracellular protease produced were investigated.
Of the media experimented, medium-D composed of yeast extract 1%, peptone 1%, NaCl 1%, K2HPO4 1% and casein 2% was found to be the most preferable for the production of the extracellular protease. The extracellular protease was prepared from medium-D after 24 hours' growth of Brev. linens at 20°C by ammonium sulfate precipitation. Protease was purified ca. 18 times above that of the original enzyme (culture filtrate) by Sephadex G-100 column chromatography, and enzymatic properties of it were studied.
The optimum pH of the protease was 7.0 in phosphate buffer. The optimum temperature was 25°C, and the inactivation of the extracellular protease was observed to begin already even at 40°C, and ten minutes' heating at 50°C resulted in camplete loss of activity. The extracellular protease hydrolyzed actively milk casein and bovine haemoglobin, while unheated egg albumin was slightly hydrolyzed, and egg albumin heated at 95°C for 10 minutes was hardly hydrolyzed by this protease.View full abstractDownload PDF (420K) -
[in Japanese], [in Japanese], [in Japanese], [in Japanese]1972 Volume 43 Issue 1 Pages 49-50
Published: January 25, 1972
Released on J-STAGE: March 10, 2008
JOURNAL FREE ACCESSDownload PDF (606K)
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