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Volume 70 (1971)
- Issue 6 Pages 885-
- Issue 5 Pages 723-
- Issue 4 Pages 549-
- Issue 3 Pages 375-
- Issue 2 Pages 205-
- Issue 1 Pages 1-
Volume 70, Issue 6
Displaying 1-21 of 21 articles from this issue
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I. Vaporization of a Mercury Compound from Mercuric Chloride by Multiple Drug Resistant Strains of Escherichia coliIchiro KOMURA, Kazuo IZAKI1971Volume 70Issue 6 Pages 885-893
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThree strains of Escherichia coli possessing the multiple drug resistance were found to be resistant also to HgCl2, though they were sensitive to other heavy metal ions such as nickel, cobalt, cadmium and zinc ions. Like the resistance to drugs such as chloramphenicol and tetracycline, the HgCl2 resistance could be transferred from a resistant strain of E. coli to sensitive strains of E. coli and Aerobacter aerogenes. The resistant strains could grow in the presence of 0.02mM HgCl2, whereas a sensi-tive strain failed to grow in the presence of 0.01mM HgCl2. During cultivation in the presence of HgCl2, the cells of resistant strain vaporized a form of radioactive mercury when incubated with 203HgC12, glucose and NaC1 in phosphate buffer while the cells of sensitive strain showed no such activity. This phenomenon seemed to explain the HgCl2 resistance of the resistant strains.View full abstractDownload PDF (750K) -
II. NADPH-Dependent Reduction of Mercuric Chloride and Vaporization of Mercury from Mercuric Chloride by a Multiple Drug Resistant Strain of Escherichia coliIchiro KOMURA, Tsukasa FUNABA, Kazuo IZAKI1971Volume 70Issue 6 Pages 895-901
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe activity to vaporize a 203Hg compound from 203HgCl2 was demonstrated in crude cell-free extracts of a strain of Escherichia coli W2252, which had acquired the multi-ple drug resistance. NADPH was essential for the vaporization, while NADH had only a slight stimulating effect and NADP+ had no effect. The oxidation of NADPH dependent on HgCl2 was also demonstrated in the crude extracts, but the HgCl2-dependent NADH oxidation could be demonstrated only when a partially purified enzyme preparation was used. The rate of NADH oxidation was much slower than that of NADPH oxidation. It was concluded that NADPH, and to a lesser extent NADH, act as electron donors for the enzymatic reduction of HgCl2, and the vapori-zation occurs after this reduction. This reduction and subsequent vaporization seem to provide a mechanism of resistance to HgCl2 in E. coli strains having the multi-ple drug resistance.View full abstractDownload PDF (597K) -
Junji HASHIMOTO, Tsuneko UCHIDA, Fujio EGAMI1971Volume 70Issue 6 Pages 903-911
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. RNase U1 was highly purified from the culture media of Ustilago shhaerogcyna. The purified enzyme was demonstrated to be homogeneous by chromatography on Sephadex G75, disc gel electrophoresis and C-terminal amino acid analysis.
2. Some similarities were recognized in amino acid compositions of RNases U1, N1 and T1, and all three RNases had four residues of half cystine. Unlike RNases T1 and N1, RNase U1 had no tryptophan residue.
3. The amino terminal of RNase N1 was determined to be alanine and the carboxyl terminal of RNase U1 was determined to be tyrosine.
4. In the hydrolysis of guanosine 2', 3'- cyclic phosphate, 5- to 10-fold amounts of RNase N1 was necessary to obtain the same degree of hydrolysis to that by RNases U1 and T1.
5. When RNases U1 and N1 were treated with a large excess of iodoacetate at pH 5.5, these enzymes were inactivated at the similar rate of the inactivation of RNase T1.View full abstractDownload PDF (1165K) -
Tamaichi ASHIDA, Tatzuo UEKI, Tomitake TSUKIHARA, Akio SUGIHARA, Tsune ...1971Volume 70Issue 6 Pages 913-924
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe crystal structure of bonito ferrocytochrome c has been studied at 4Å resolution on the basis of two isomorphous heavy atom derivatives (K3UO2F5 and K2PtCl4). The crystal of bonito ferrocytochrome c belongs to an orthorhombic system with a space group of P212121. The unit cell dimensions are: a=57.54, b=84.71 and c=37.74Å. The crystal contains two kinds of molecules which are nearly equivalent to each other via the pseudo-twofold axis along the a axis.
The main structural features of bonito ferrocytochrome c molecule, such as the size and shape, the pathway of the polypeptide chain, and the orientation and the environment of the heme group, appear to be similar to those of;horse ferricyto-chrome c, although it is suggested that the side-chain conformation' at the surface of ferrocytochrome c is different from that of ferricytochrome c. The molecule is a prolate spheroid of a dimension of about 30×30×35Ä. Its heme group sits in the center of the molecule, with one corner exposed to the surroundings. In the crystal, the molecules are in close contacts with one another; usually, the residues present in the contact regions have long polar side chains.
In the crystal, the PtCl42- ion is located closely at Met 65 as in the case of horse ferricytochrome c. The reagent, K2HgI4, deteriorates the crystal structure, and it cannot be used for the structure analysis. On a difference Fourier map, however, the Hg group is located closely at Cys 17, which links the heme group to the polypeptide chain.View full abstractDownload PDF (1588K) -
II. Accidentally Modified Kunitz Soybean Trypsin InhibitorShoji ODANI, Takehiko KOIDE, Tokuji IKENAKA1971Volume 70Issue 6 Pages 925-936
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA soybean trypsin inhibitor (Kunitz) whose several amino acid residues such as methionine. tryptophan and tyrosine were modified was obtained during the purifi-cation of the trypsin inhibitor from soybean flakes, and the properties and modified amino acid residues of the inhibitor were investigated.
1. This inhibitor was separated into monomer, dimer and polymer by gel filtration, and the monomer and the dimer had 83 and 40%, respectively, of the inhibitory activity of the native inhibitor.
2. The modified residues were methionines at residues 100 and 130, tryptophan at 133 and tyrosines at 17 and/or 18.
3. Two methionines were oxidized to methionine sulfoxide, a part of tyrosines-17 and/or -18 was chlorinated to monochlorotyrosine and tryptophan-133 was modified into unknown forms.
4. It was deduced that the modification of these amino acid residues in the protein had been caused by chlorine during dialysis of the protein against tap water.View full abstractDownload PDF (906K) -
Susumu YASUOKA, Setsuro FUJII1971Volume 70Issue 6 Pages 937-944
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSEsterase and lipase activities were determined with tributyrin and Ediol as substrate, respectively. Both activities were released into the blood by intravenous injection of heparin. The postheparin esterase and lipase (clearing factor lipase, CFL) activities were not separated from each other by gel filtration on Sephadex G-200 and Sepharose 4B.
CFL was purified 2, 000-fold by a modification of the method of Fielding. It catalyzed the hydrolysis of tributyrin as well as that of Ediol. The activity ratio of lipase to esterase of the preparation after Sephadex G-200 filtration was the same as that of purified CFL. Tributyrin competitively inhibited the hydrolysis of Ediol by the preparation after Sephadex G-200 filtration and by purified CFL. The esterase activity observed after heparin injection was eliminated by the antibody to CFL whereas that before heparin injection was not. The esterase activity after heparin injection was inhibited by sodium chloride as much as CFL activity.
From these results it was concluded that CFL catalyzes the hydrolysis of glycerides of both short- and long-chain fatty acids, and that the increase in the esterase activity in the plasma after heparin injection is caused by the esterase activity of CFL.View full abstractDownload PDF (593K) -
XVII. Isolation and Amino Acid Sequences of Papain and Subtilisin Peptides from Ribonuclease T1-The Complete Covalent Structure of Ribonuclease T1Kenji TAKAHASHI1971Volume 70Issue 6 Pages 945-960
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSRibonuclease T, [EC 2. 7. 7. 26] (about 4 to 5μmoles) was hydrolyzed separately with 2% by weight of papain at pH 5.8 and 37°C for 24hr and with 1% by weight of subtilisin (Nagarse) at pH 8.0 and 37°C for 5 hr. The digests were submitted sepa-rately to the chromatographic and electrophoretic separations by essentially the same procedures as employed in the preceding experiments.
In this way nearly 20 peptides each were isolated and identified, accounting for about one-half and two-thirds, respectively, of the residues in the entire chain. All these peptides fit the amino acid sequence of the protein established already (1-4 ). The validity of the alignment of the chymotryptic and the peptic peptides which had led to derivation of the complete amino acid sequence of the protein (4) was supported further by isolation of an overlapping peptide from the papain digest which comprises residues 48 to 51.
In the subtilisin peptides, two major cystine-containing peptides were found. From the analyses after performic acid oxidation, their structures were deduced to be_??_
Thus the arrangement of the two disulfide bonds in the intact protein was eluci-dated, and hence the complete covalent structure of ribonuclease T, has been esta-blished.View full abstractDownload PDF (994K) -
Takao MAKAMURA1971Volume 70Issue 6 Pages 961-966
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA design of a new flow apparatus is presented. This new flow apparatus, which is characterized by steadiness of the flow of various speeds, small dead volume and good time resolution, is rather simple and is satisfactory for both steady and stopped flow determinations. Spectrophotometric as well as other detector systems are ap-plicable. The minimum dead time for optical measurements is 0.45msec at the flow speed of 650cm/sec.View full abstractDownload PDF (2597K) -
Michio OGURA, Junichi SHIGA, Kazumi YAMASAKI1971Volume 70Issue 6 Pages 967-972
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAfter rats with bile fistulas were injected with either [4-14C]cholesterol or [4-14C]-cholesteryl oleate, or with a mixture of [1, 2-3H]cholesterol and DL-[2-14C]mevalonate, biliary bile acids and cholesterol in both liver and serum were separated by chroma-tography and analyzed. The data obtained suggested that the immediate precursor of bile acids was the free cholesterol but not the esterified one and that both cholic and chenodeoxycholic acids originated from a common precursor cholesterol pool.View full abstractDownload PDF (444K) -
Influence of Molecular Structures of Substrates and Analogues on Taka-amylase A Catalyzed HydrolysesIII. Inhibition by 2-Deoxy-D-glucose and Methyl α-D-Glucoside: Change in Inhibition Type with Substrate Chain LengthYasunori NITTA, Keitaro HIROMI, Sôzaburo ONO1971Volume 70Issue 6 Pages 973-979
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The inhibitory effects of 2-deoxy-D-glucose, methyl α-D-glucoside and D-gluco-samine on the hydrolytic reaction catalyzed by Taka amylase A [EC 3. 2. 1. 1] were studied at 25°C and pH 5.3 using phenyl-α-maltoside and linear oligosaccharides as substrates. These analogues were previously reported to inhibit the hydrolysis of phenyl α-maltoside noncompetitively (1). 2. In inhibition studies, with a mixture of the analogues which inhibited hydrolysis of phenyl α-maltoside noncompetitively these analogues were found to compete with each other for the same site (termed the site N) on the enzyme. 3. In similar studies with a mixture of a noncompetitive inhibitor (2-deoxy-D-glucose or methyl α-D-glucoside) and a competitive inhibitor (D-glucose or D-xylose) no inter-action was detected between the site N and the binding site of the competitive in-hibitors. 4. However, when the naturel linear oligosaccharides, maltotetraose and malto-heptaose are used as substrates, the analogues which inhibited hydrolysis of phenyl α-maltoside noncompetitively were found to exhibit competitive inhibition. The lo-cation of the site N in the specificity region of this enzyme was proposed on the basis of the effect of the chain length of linear substrates on this alteration of in-hibition type, and on previous results on subsite affinities (2).View full abstractDownload PDF (477K) -
I. Intracellular Distribution of Oxidative Enzymes in Lung CellsTakashi MATSUBARA, Yoshihiro TOCHINO1971Volume 70Issue 6 Pages 981-991
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSRabbit lung cells were homogenized in 0.15M KCl containing 10mM phosphate buffer, pH 7.4, and the homogenate was fractionated by differential centrifugation. The distribution patterns of chemical components and oxidative enzymes in lung subcel-lular fractions were similar to those in liver cells. Lung mitochondria (Fraction II) showed a cytochrome pattern characteristic for the mitochondrial respiratory chain, but the contents of cytochromes were only about one fifth those in liver mitochondria. Lung microsomes (Fraction III) contained cytochromes b5 and P-450 as well as NADH-and NADPH-cytochrome c reductase activities. The contents of the cytochromes and the specific activities of the reductases were, however, one third to one fifth the levels reported for liver microsomes. The NADH-reduced minus oxidized differ-ence spectrum of lung microsomes, representing the difference spectrum of cyto-chrome b5, was slightly different from that of liver microsomes.View full abstractDownload PDF (858K) -
I. Purification and Some Properties of the EnzymeAkihiko NOMURA, Masahiro SUNO, Yoshihisa MIZUNO1971Volume 70Issue 6 Pages 993-1001
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSAn enzyme having both 3'-nucleotidase and nuclease activities was purified from potato tubers by ammonium sulfate fractionation, heat treatment, dialysis at pH 6.0 and chromatography on phosphocellulose. The 3'-nucleotidase and the nuclease activities were purified 1140-, and 750-fold, respectively. The enzyme dephosphorylated ribonucleoside 3'-phosphates and their 5'-substituted derivatives, and hydrolyzed RNA, DNA and synthetic polyribonucleotides. Attempts to separate the two activities by several physical and chemical means were unsuccessful. It is suggested that a single enzyme is responsible for both types of hydrolysis.View full abstractDownload PDF (665K) -
Masahiro OHATA, Hajime ORIMO, Takuo FUJITA, Masaki YOSHIKAWA1971Volume 70Issue 6 Pages 1003-1010
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSA method of assay for inorganic pyrophosphatase [EC 3. 6. 1. 1] using 32P-labeled pyrophosphate was developed especially for the purpose of assaying bone tissue. Rat tissues were found to have inorganic pyrophophatase activity with optimal pHs at 2.5 (acid PP.ase) and 7.5 (alkaline PP ase). The alkaline PP ase but not acid PP ase was activated by Mg2+, Ca2+, Co2+ and Zn2+. Both PP ases appear to be SH-enzymes in view of the inhibition by iodoacetate, p-chloromercuribenzenesulfonic acid and Hg2+.View full abstractDownload PDF (656K) -
Kikuko TAKEUCHI, Yuji TONOMURA1971Volume 70Issue 6 Pages 1011-1026
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. The binding ratios of heavy meromyosin (HMM) and subfragment-1 (S-1) of myosin to F-actin were measured by light-scattering and ultracentrifugal methods. The ratios were one mole of HMM per mole of actin dieter with a dissociation constant of 1.6-2.6×10-7M and one mole of S-1 per mole of actin monomer. They were not affected by the method of preparation of actin or the KCI and MgCl2, con-centrations. The distribution of HMM on the F-actin filament was analyzed by electron microscopy. Some acto-H-meromyosin preparations showed a random dis-tribution of HMM on F-actin, while others showed a distribution suggesting cooper-ative binding of HMM to F-actin.
2. The amounts of the initial burst of P1-liberation from the HMM-ATP and the S-1-ATP systems were one mole and 0.5 mole per mole of protein, respectively. The values were not affected by ionic strength.
3. The decrease in light-scattering intensity after adding ATP to acto-HMM or acto-S-1 complexes was measured by a stopped flow method. The minimum amounts of ATP required for the maximum decrease in light-scattering intensity were 2.2 moles and 1.0 mole per mole of HMM and S-1, respectively.
4. From these results it was concluded that each of the two head parts of HMM has one binding site for actin, and that the binding of one site with actin is dis-sociated by formation of the HMM-phosphate-ADP complex, while the binding of the other site is broken by simple binding of ATP.View full abstractDownload PDF (1912K) -
Toshiaki ABE, Shizuo HANDA, Tamio YAMAKAWA1971Volume 70Issue 6 Pages 1027-1033
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSβ-N-Acetylhexosaminidase which contained no α-N-acetylhexosaminidase was prepared from hog epididymis. Several sphingoglycolipids containing N-acetylhexosamine were examined as substrates for this enzyme.
Globoside I (Ga1NAc-Gal-Gal-Glc-ceramide) and “Tay-Sachs Globoside” (Ga1NAc-Gal-Glc-ceramide) were hydrolyzed by this enzyme. The optimal pH was 4.2 and the half maximal velocity was obtained at 3.7×10-3M for Globoside I. Globoside, which was obtained from horse kidney and sheep erythrocytes and carried Forssman hapten activity, and glycolipids containing no hexosamine at the non-reducing terminal and G_??_2-ganglioside_??_were not hydrolyzed by this enzyme.View full abstractDownload PDF (1094K) -
Partial Purification and Properties of O-Acetylhomoserine SulfhydrylaseShuzo YAMAGATA1971Volume 70Issue 6 Pages 1035-1045
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSO-Acetylhomoserine sulfhydrylase, catalyzing the synthesis of homocysteine from O-acetylhomoserine and hydrogen sulfide, was purified more than 100-fold from baker's yeast mainly by means of DEAE-cellulose column chromatography. Polyacrylamide gel electrophoresis revealed that the purified preparation consisted of at least three protein components, of which only the main component possessed the sulfhydrylase activity. As revealed with Neurospora enzyme, this enzyme also required O-acetyl-L-homoserine as a substrate, but pyridoxal 5-phosphate was required for its activity. The Km, values of the enzyme for O-acetyl-L-homoserine and pyridoxal 5-phosphate were determined to be 4.55×10-3M and 2.94×10-5M, respectively. Hydrogen sulfide could be replaced by methyl and ethyl mercaptans giving rise to methionine and ethionine, respectively. Cystathionine was not synthesized froze O-acetylhomoserine and cysteine in the presence of the enzyme. O-Acetyl-L-serine (K1=21.8mM), O-succinyl-DL-homoserine (K1=19.0mM), L-homoserine (K1=16.0mM) and L-methionine (K1=0.9mM) inhibited the enzyme in competition with O-acetylhomoserine.View full abstractDownload PDF (1487K) -
III. Self-assembly of Sheath SubunitsChie YUI-FURIHATA1971Volume 70Issue 6 Pages 1047-1050
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
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Junzo KATO, Yachiyo ATSUMI, Machiko INABA1971Volume 70Issue 6 Pages 1051-1053
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (180K) -
Koki YOKOTSUKA, Aiko KIKUCHI, Kensuke SHIMURA1971Volume 70Issue 6 Pages 1055-1059
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
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Akio ITO1971Volume 70Issue 6 Pages 1061-1064
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (324K) -
Fumio WADA, Michiyuki USAMI, Masanobu GOTO, Takahiko HAYASHI1971Volume 70Issue 6 Pages 1065-1067
Published: December 25, 1971
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (234K)
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