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Volume 66 (1969)
- Issue 6 Pages 751-
- Issue 5 Pages 573-
- Issue 4 Pages 431-
- Issue 3 Pages 289-
- Issue 2 Pages 123-
- Issue 1 Pages 11-
Volume 66, Issue 5
Displaying 1-21 of 21 articles from this issue
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YASUHARU TSUZUKIDA, SATOKO ISEMURA, TAEKO KITANO, KUNIO MATSUI1969 Volume 66 Issue 5 Pages 573-579
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSMethionine tRNA of baker's yeast was fractionated into two fractions, I and II, which were partially purified (53 and 37% respectively) by a combination of known chromatographic methods. Methionyl-tRNA I was formylated by formyltransferase [EC 2. 1. 2] from E. coli, whereas II was not. The latter was more labile than the former.View full abstractDownload PDF (520K) -
KUNIO YAGI, KENTARO OKAMURA, MAKOTO NAOI, AKIKO TAKAI, AKIRA KOTAKI1969 Volume 66 Issue 5 Pages 581-589
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSOxidation of D-lysine by D-amino-acid oxidase [EC 1. 4. 3. 3] has been demonstrated by observing the stoichiometric relation between oxygen consumed and D-lysine oxidized. The enzymatic reaction is considerably influenced by the ionization of ε-NH3+ group of the substrate. At pH 8.3, the oxidation of D-lysine is slow and is accompanied by a typical product inhibition, because the enzyme forms a stable complex with Δ1-piperidine-2-carboxylate which is furnished by spontaneous cyclization of α-oxo-ε-amino-caproate, the direct product of the enzymatic reaction. When the pH is raised to 10, however, such inhibition disappears, and the enzyme shows the maximal activity with D-lysine. In the absence of oxygen, a purple intermediate accumulates. Studies of visible absorption, ORD and ESR measurements have shown that this purple complex is essentially identical with the ‘inner complex’ of this enzyme with D-alanine. On denaturation of the apoenzyme moiety of the complex with 12N H2SO4, the coenzyme moiety is split to give free rhodoflavin. The acidified supernatant was found to contain a significant amount of D-pipecolic acid, a potential substrate of this oxidase. The mechanism of the conversion of D-lysine to D-pipecolate is discussed from the viewpoint of the reversibility of this enzymatic reaction under anaerobic conditions.View full abstractDownload PDF (1208K) -
HISATAKA KASAI, KENJI TAKAHASHI, TOSHIO ANDO1969 Volume 66 Issue 5 Pages 591-597
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Ribonuclease T1 [EC 2. 7. 7. 26] was treated with 100-fold molar excess of trinitrobenzenesulfonate at pH 7.7 and 15°C. About one equivalent of trinitrophenyl group was introduced into the protein fairly rapidly. The initial rate of the reaction was dependent on the concentration of phosphate ions in the medium and further re-action proceeded much more slowly.
2. After 83-hour reaction, a single derivative was obtained, which was homogeneous on electrophoresis and contained two trinitrophenyl groups per molecule. Chemical analyses showed that two amino groups in the protein (α-amino group of Ala-1 and ε-amino group of Lys-41) were quantitatively trinitrophenylated without changes in other amino acid residues.
3. This modified enzyme possessed 67% of the original enzymatic activity toward RNA at pH 7.5. The optimum pH for the enzymatic activity shifted slightly (by about 0.5 pH unit) toward acidity by trinitrophenylation. The modified enzyme had a Km value similar to that of the native enzyme, and a Vmax value about 60% of that of the native enzyme. The modified protein showed decreased stability and solubility.
4. These results show clearly that the two amino groups in ribonuclease T1 are not essential for the enzymatic activity, though these positively charged groups may, to some extent, contribute to the maintenance of a stable conformation of the protein.View full abstractDownload PDF (492K) -
X. The Reaction Mechanism of the Myosin-ATP System and a Molecular Mechanism of Muscle ContractionYUJI TONOMURA, HIROSHI NAKAMURA, NAOKAZU KINOSHITA, HIROFUMI ONISHI, M ...1969 Volume 66 Issue 5 Pages 599-618
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. With ITP as substrate, the initial burst of Pi-liberation was about 1 mole/4×105g of myosin at high concentrations of MgCl2 (1-10mM), but it decreased with decrease in the concentration of MgCl2 below 1mM.
2. The time-course of TCA-labile 32Pi-liberation from the myosin-γ-32P-ATP system was measured after adding the stoichiometric amount of γ-32P-ATP to myosin, together with various amounts of ITP, deoxy-ATP or ADP. The amount of initial burst of 32Pi-liberation decreased with increase in the concentration of ITP, deoxy-ATP or ADP, but its initial rate was not affected by adding ATP analogues.
3. The initial rapid liberation of H+ after mixing the stoichiometric amount of ATP with myosin was measured using a stopped-flow method. The rate of the initial rapid H+-absorption was too fast to be observed by this method.
4. In addition to the rapid stoichiometric H+-liberation, a slow stoichiometric liberation was observed with a pH-stat after adding the stoichiometric amount of ATP to myosin. The rate constants of the slow liberation were 0.7 and 0.4min-1, respectively, in 0.5 and 2.8M KCl. The rate in 0.5M KCl was much lower than that after adding a large amount of ATP. The rate in 2.8M KCl was almost equal to the initial rate after adding a large amount of ATP, but the latter decreased gradually to that in the steady state.
5. The time-course of change in optical density at 293mμ after mixing the stoichiometric amount of ATP with myosin was equal to that of the initial rapid H+-liberation under the same conditions.
6. When the stoichiometric amount of ATP was mixed with myosin, the ultraviolet spectrum of myosin changed rapidly, as mentioned above, and then the change decayed gradually. The time for half maximum decay, τ1/2, was about 50 sec. This value was in good agreement with the τ1/2 value for ADP-liberation from the myosin-phos-phate-ADP complex, _??_
7. The amount of change in the spectrum of myosin induced by ATP remained constant between pH 6.0 and 9.5. The value of τ1/2 of the decay was maximal at pH 7.5 and decreased on both acidic and alkaline sides. The value of τ1/2 increased with increase in the KCl concentration.
8. When myosin was incubated with NTP*** for 2hr in the presence of 2mM ATP, 0.6M KCl and 10μM MgC12, 2 moles of NTP were bound to 4×105g of myosin and the extra-burst was completely inhibited. However, the stoichiometric initial burst of Pi-liberation and the ATPase activity in the steady state were unaffected, and the ability of myosin to bind to F-actin was preserved.
9. ATP did not induce superprecipitation of actomyosin reconstituted from F-actin and NTP(2)-myosin produced by the method described above. The ATPase activity of actomyosin was slightly inhibited in 0.05M KCl, 10μM MgCl2 and 0.4mM ATP, and markedly inhibited in 0.01M KCl, 10μM MgCl2 and 0.1mM ATP, by treatment of myosin with NTP.
10. On the basis of the reaction mechanism of the myosin-ATP system described in this series of papers, a molecular mechanism of muscle contraction was proposed: sliding of F-actin filaments past myosin filaments is induced by a conformational change of myosin coupled with the cyclic phosphorylation and dephosphorylation of myosin, and by the dissociation of actomyosin caused by formation of the myosin-phosphate-ADP complex, _??_. Which of these two reactions occurs depends on the conformation of myosin.View full abstractDownload PDF (3848K) -
MASARU KAWAMURA, KOSCAK MARUYAMA1969 Volume 66 Issue 5 Pages 619-626
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe particle lengths of natural and reconstituted actomyosins were measured by electron microscopy and compared with the values obtained in solution by the flow birefringence technique.
The particle lengths of natural actomyosin (myosin B) were fairly homogeneous: the number-average length (<L>n) was about 0.5μ and the weight-average length (<L>w) was about 0.66μ.
On the other hand, the particle lengths of reconstituted actomyosin were heteroge-neous like those of F-actin. However, the value of <L>n of 0.52μ and that of <L>w of 0.98μ, were much shorter than those of the F-actin used to form actomyosin. The length of myosin-free F-actin was still shorter. The mechanism of the change in particle length is discussed.
Particle lengths calculated from flow birefringence data were much longer than those measured by electron microscopy. This difference is discussed.View full abstractDownload PDF (2319K) -
TAKESHI NEMOTO, ZENSAKU YOSIZAWA1969 Volume 66 Issue 5 Pages 627-636
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A glycopeptide and three acidic glycosaminoglycan (mucopolysaccharide)-peptides were obtained from the protease-digested gastric mucosa of rabbit.
2. Separation of these four polymers was achieved by stepwise elution from DEAE-Sephadex A-25 with increasing concentration of NaCl in 0.01 N HCl. The glycopeptide was purified by rechromatography on Dowex 1-×2, followed by gel filtration on Sephadex G-200. Nucleic acid-like substance was removed from the acidic glycosaminoglycan-peptides by gel filtration on Sephadex G-50. They were further purified by zone electrophoresis on GEON.
3. Homogeneity of the purified fractions was shown by ultracentrifugation, paper electrophoresis, zone electrophoresis and gel filtration.
4. All the purified preparations contained galactose, glucosamine, galactosamine and peptide as the major constituents, with small amounts of fucose and very minute amounts of mannose and glucose. A small amount of sialic acid was found in the glycopeptide, in addition to the above constituents. As the other major constituents, sialic acid and uronic acid were also found in an acidic glycosaminoglycan-peptide (fraction 0.5), while uronic acid and sulfate in the remaining two acidic glycosaminoglycan-peptides (fractions 0.7 and 1.0).
5. Threonine, proline and serine were the predominant amino acids in all the purified preparations. The results of the alkali treatment suggest the linkages through the hydroxyl group of threonine and serine to carbohydrates.
6. A possible hybridity of the three acidic glycosaminoglycan-peptides is discussed.View full abstractDownload PDF (2105K) -
TOMOH MASAKI, OSASI TAKAITI1969 Volume 66 Issue 5 Pages 637-643
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. A simple method for preparation of chicken α-actinin was described.
2. According to electrophoretic and amino acid analyses, the light component (the 6S component) of α-actinin was an entirely different protein from the middle component (the lOS component) or from actin, whereas no definite evidence was presented to discriminate the middle component from actin.
3. The accelerating effect of α-actinin on the superprecipitation belonged solely to the light component.
4. The sedimentation coefficient of the light component of α-actinin in a solution of low ionic strength showed a concentration dependence and its s020, W was 6.8S. When the ionic strength of the medium was increased, the light component of α-actinin split into two peaks, of which the apparent sedimentation coefficients were approximately 7S and 12S respectively at a protein concentration of 3.5mg/ml. The latter component seemed to be the associated form of the former component.View full abstractDownload PDF (1878K) -
IWAO OHTSUKI1969 Volume 66 Issue 5 Pages 645-650
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The microsome fraction from dog brain accumulated Ca ions in the presence of Mg-ATP. The amount of Ca taken up by the microsomes was 40-80μmoles/g protein.
2. The characteristics of the Ca uptake of dog brain microsomes were essentially the same as those of rabbit muscle microsomes, but the former Ca uptake was much slower in rate and dependent upon temperature more pronouncedly.
3. Respiratory substrates and metabolic inhibitors did not influence the Ca uptake of brain microsomes. It was concluded that the component responsible for the Ca uptake was different from mitochondria or their subfragments.
4. Brain microsomes showed a Mg-ATPase [EC 3. 6. 1. 3] activity, the properties of which were similar to those of muscle microsomes, and also showed a Na-K-ATPase activity in the presence of azide.
5. The Ca uptake and Na-K-ATPase activities were shown to be distributed differently when centrifuged in a discontinuous sucrose density gradient.
6. It was suggested that the Ca accumulating activity of brain microsomes should mainly be derived from the endoplasmic reticulum and play a role in maintaining the excitability of the surface membrane by lowering the intracellular Ca concentration.View full abstractDownload PDF (430K) -
TORU TAKAMI1969 Volume 66 Issue 5 Pages 651-658
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSome enzymatic properties of purified hog pancreatic kallikrein [EC 3. 4. 4. 21] were investigated. The hog pancreatic kallikrein showed the specificity towards arginine and lysine residues in its esterase activity. Benzoyl-L-arginine ethyl ester was hydrolyzed most rapidly among the investigated synthetic amino acid esters and it was followed by benzyloxycarbonyl-L-lysine benzyl ester, benzyloxycarbonyl-L-lysine methyl ester, tosyl-L-arginine methyl ester, benzoyl-L-lysine methyl ester, and so on. However, tosyl-L-methionine ethyl ester was not hydrolyzed by hog pancreatic kallikrein. The optimal pH of kallikrein was 8.5 with benzoyl-L-arginine ethyl ester. Kinetic constants for the above substrates were determined, and from the measurement of the kinetic constants on pH dependency, it was elucidated that the activity of kallikrein was dependent on the group ionizing near pH 6.5. Kallikrein was not inhibited by α-N-tosyl-L-lysine chloromethyl ketone. Metal salts except univalent cations had an inhibitory effect on the esterase activity of kallikrein.View full abstractDownload PDF (532K) -
NORIKO TAKAHASHI, YOKO YASUDA, MASAKO KUZUYA, TAKASHI MURACHI1969 Volume 66 Issue 5 Pages 659-667
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Experiments were carried out to determine the amino acid sequence of a glyco-peptide isolated from pineapple stem bromelain [EC 3. 4. 4. 24]. Phenylthiocarbamylation of the glycopeptide unexpectedly revealed heterogeneity of the preparation used, leading to separation of four closely related glycopeptides, X, Y-l, Y-2, and Z, upon paper electrophoresis and paper chromatography.
2. The four glycopeptides were isolated and their amino acid sequences were established: Asn(sugar)-Glu-Ser for peptide X, Asn-Asn(sugar)-Glu-Ser for Y-1, Asn (sugar)-Glu-Scr-Ser for Y-2, and Asn-Asn(sugar)-Glu-Ser-Ser for Z. The relative yields of peptides X, Y-1, Y-2, and Z were 1.0, 0.14, 0.29, and 0.38 respectively. From the comparison among these sequences, together with the specificity of the proteinase used for the digestion, it was concluded that peptides X, Y's, and Z were simultaneously derived from the same portion of the parent stem bromelain molecule.
3. In each of the four glycopeptides isolated an asparaginyl residue was shown to exist as the branching point to the carbohydrate moiety. Phenylthiohydantoin deriva-tives of the carbohydrate-asparagine complex were isolated and identified. Additional evidence was also provided to indicate that the structure of the carbohydrate-peptide linkage is that of glycosylamine type involving the anomeric carbon atom of N-acetyl-glucosamine and the β-amide nitrogen atom of asparagine.View full abstractDownload PDF (684K) -
HACHIRO NAKAGAWA, HIROSHI KIMURA1969 Volume 66 Issue 5 Pages 669-683
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSSerine dehydratase [EC 4. 2. 1. 13] was crystallized from rat liver. Crystalline enzyme was found to be homogeneous and to have an s20, W value of 4.25 by ultracen-trifugation. Its molecular weight was calculated to be 64, 000 by the sedimentation equilibrium method.
In the Ouchterlony gel double diffusion test, crystallized enzyme behaved as a single band against the anti-serine dehydratase serum obtained from rabbits immunized with the same preparation.
Crystallized enzyme moved as a single component on pH gradient electrophoresis and its isoelectric point was determined to be pH 6.7. However, the preparation was separated into two fractions by starch zone electrophoresis.
The possibility that threonine dehydratase [EC 4. 2. 1. 16] differed from serine dehydratase in rat liver was excluded by the following results;
1) The ratio of serine dehydratase to threonine dehydratase was constant at all steps of purification of serine dehydratase.
2) Crystallized enzyme was separated into two fractions, but the ratios of serine dehydratase to threonine dehydratase in the two fractions were the same.
3) Anti-serine dehydratase serum inhibited threonine dehydratase activity to the same extent as serine dehydratase activity.
4) L-Threonine inhibited serine dehydratase competitively.
On the other hand, the following results show that serine dehydratase differs from cystathionine synthetase;
1) Anti-serine dehydratase serum inhibits serine dehydratase, but not cystathionine synthetase activity.
2) The two enzymes were separated by Sephadex G-100 column chromatography. The Km values for L-serine and L-threonine were determined to be 5.7×10-2M and 8.7×10-2M, respectively.
It was shown that the enzyme requires pyridoxal phosphate and a sulfhydryl com-pound. The dissociation constant of pyridoxal phosphate was calculated to be 3.7×10-7M. Crystallized enzyme contained 2 moles of pyridoxal phosphate per mole.
Serine dehydratase was strongly inhibited by DL-selenocystine. The toxicity of seleno-compounds in higher animals was discussed in relation to our findings.View full abstractDownload PDF (3265K) -
IWAHIKO YAMAMOTO, MICHIHIRO SUGANO, AKIHIKO KADOTA, YOSHICHIKA SATO, M ...1969 Volume 66 Issue 5 Pages 685-691
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSTriglycerides containing similar amounts of essential fatty acids (EFA) (approxi-mately 53% of the total fatty acids) but different fatty acid configurations on the gly-cerides were prepared from soy bean oil and fat from a pig fed on a 20% safflower oil ration. The vegetable oil contained approximately 48% of the total EFA at the 2-position, while the pig fat contained only 27% at this locus. Diet containing 5% (w/w) soy bean oil or pig fat were supplied ad libitum to two groups of male weanling rats for 3, 6 and 13 weeks.
After these periods there was no difference in the concentration of plasma choles-terol in the two groups. The liver cholesterol level tended to increase when rats received pig fat for longer periods.
In the group receiving pig fat, addition of 1% cholesterol to the diet resulted in a considerable increase in the plasma and liver cholesterol levels and the ratio of esterified to total cholesterol in the liver increased to above that in the group receiving vegetable oil plus cholesterol.
These data suggest that the effect of dietary EFA on the metabolism of cholesterol differs with the position of the esterified EFA on the glyceride. Thus, EFA at the 1- and 3-positions on triglycerides may have less effect in lowering the cholesterol level than EFA at the 2-position, particulary when cholesterol is ingested simultaneously.View full abstractDownload PDF (485K) -
V. Interaction with α-Actinin, Tropomyosin and Native TropomyosinHIROKO HAMA, KOSCAK MARUYAMA1969 Volume 66 Issue 5 Pages 693-698
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSComposition of natural F-actin, directly isolated from myofibrils, was investigated. The results of turbidity test showed clearly the presence of 6S component of α-actinin. When purification was repeated, the content of α-actinin was decreased, and the effect of added α-actinin became remarkable.
The Ca sensitivity of natural F-actin-myosin complex was negligible, and largely recovered by the addition of troponin, but not by tropomyosin. This fact suggests that all of troponin and some of tropomyosin were lost during the preparation procedure.
The interaction of natural F-actin with tropomyosin and native tropomyosin was studied by measurements of viscosity, flow birefringence and sedimentation. Tropo-myosin was found to bind to natural F-actin, as well as to Straub's F-actin. The sedimentation coefficient of natural F-actin was increased from 39S to 47S by the binding of tropomyosin. Natural F-actin also interacted with native tropomyosin in the same way as Straub's F-actin.View full abstractDownload PDF (1169K) -
FUMIO WADA, KAZUYA HIRATA, KAZUYASU NAKAO, YUKIYA SAKAMOTO1969 Volume 66 Issue 5 Pages 699-703
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe participation of the microsomal electron transport system involving cytochrome P-450 in 7α-hydroxylation of cholesterol by a rat liver preparation was examined since this process involves microsomal reactions requiring both NADPH and molecular oxygen.
7α-Hydroxylation of cholesterol was inhibited by carbon monoxide and by antibody against NADPH-cytochrome c reductase. The 7α-hydroxylase activity of liver microsomes in animals under various conditions varied but variation was not in parallel with variation in the microsomal cytochrome P-450 content.
It is concluded that the microsomal electron transport system, involving cytochrome P-450, functions in 7α-hydroxylation of cholesterol. The existence of a specific cytochrome P-450 for 7α-hydroxylation, i.e., multiplicity of cytochrome P-450, is suggested.View full abstractDownload PDF (343K) -
MAKOTO HORI, TAKEHIKO KUNIMOTO, JIRO SUZUKI1969 Volume 66 Issue 5 Pages 705-709
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSWhen 0.1M n-butanol was added to a culture of exponentially growing E. coli, the polysomal structure of the bacteria was lost within 2 min. This was prevented by addition of chloramphenicol. With 0.1M butanol, both RNA and protein syntheses in the bacteria were severely inhibited. On diluting the affected culture with 3 volumes of butanol-free medium, the bacteria quickly recovered their polysomal structure and resumed normal growth without any appreciable latent period. The mode of action of butanol with respect to membrane function is discussed.View full abstractDownload PDF (333K) -
NOBUKO MIYAJIMA, MUNEHIRO TOMIKAWA, TOSHISUKE KAWASAKI, IKUO YAMASHINA1969 Volume 66 Issue 5 Pages 711-732
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Rat liver microsomes were subfractionated by DOC (deoxycholate) treatment, followed by phenol extraction, gel filtration and finally ammonium sulphate precipitation, paying particular attention to removal of plasma proteins and to the behaviour of the carbohydrate components. A fraction, tentatively designated as structural protein, was obtained which was practically free of lipid, RNA and plasma proteins. Structural protein was heterogeneous and had an extremely high molecular weight, but after reduction and carboxymethylation it gave a broad, but essentially single peak with a much lower molecular weight in gel filtration and density gradient centrifugation.
2. Immunological studies demonstrated that structural protein contained no plasma protein contaminants, except for a trace of γ-globulin, which was possibly specifically associated with microsomes.
3. Structural protein was a glycoprotein with a carbohydrate content of approximately 1.5%, made up of mannose, galactose, glucose, hexosamines and sialic acid. The small amount of inositol detected was possibly due to phosphoinositides. The molar ratio of mannose to galactose was 2.15:1, and the hexosamines consisted of both glucosamine and galactosamine in a ratio of 12.1:1. This composition appears to be membrane specific, being different from that of either plasma proteins or whole microsomes.
The amino acid composition was determined and compared with that of other membranous proteins.View full abstractDownload PDF (5423K) -
CHIAKI SHIOZAWA1969 Volume 66 Issue 5 Pages 733-735
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (143K) -
HIROSHI YOSHIDA, MASAHIRO SHIBATA1969 Volume 66 Issue 5 Pages 737-738
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (121K) -
RYUICHI KATO, AKIRA TAKANAKA, KINICHI ONODA1969 Volume 66 Issue 5 Pages 739-741
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (244K) -
YOSHIKO HARAHASHI, JUNKO FUKUNAGA1969 Volume 66 Issue 5 Pages 743-745
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (194K) -
MAKOTO KANEDA, IKUNOSHIN KATO, NAOTOMO TOMINAGA, KOITI TITANI, KOZO NA ...1969 Volume 66 Issue 5 Pages 747-749
Published: November 25, 1969
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (164K)
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