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Volume 67 (1970)
- Issue 6 Pages 753-
- Issue 5 Pages 611-
- Issue 4 Pages 507-
- Issue 3 Pages 333-
- Issue 2 Pages 157-
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Volume 67, Issue 6
Displaying 1-15 of 15 articles from this issue
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ICHIJIRO ISHIKAWA, YOSHIO UENO, HIROSHI TSUNODA1970 Volume 67 Issue 6 Pages 753-758
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSStudies were made on the chemical determination of a chlorine-containing peptide, a hepatotoxic mycotoxin of Penicillium islandicum Sopp, with the following results;
1. The ammonolysis reaction could be used in photometric determination of the peptide.
2. The peptide was adsorbed on charcoal treated with 1N HCl and could be eluted by methanol.
3. Gel filtration on Sephadex LH-20 with methanol-water (1:1, by vol.) separated the peptide from other materials lyzed by ammonia.
4. A method involving a combination of adsorption on charcoal, gel filtration and photometry was developed to fractionate and detect the peptide produced in the culture filtrate of the fungus.View full abstractDownload PDF (363K) -
KAZUO SHISHIDO, YONOSUKE IKEDA1970 Volume 67 Issue 6 Pages 759-765
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDNA's from various sources were denatured by heating and then treated at a low temperature with nuclease Si which specifically attacks single stranded DNA. 0.3-3% of the denatured DNA's were found to be resistant to the nuclease. The percentage of resistant fraction diversed considerably depending on the reaction temperature and ionic strength in the reaction mixture. The polynucleotide segments isolated from the digest by the DEAF-cellulose column chromatography exhibited thermal denaturability and high degree of renaturability. The segments were comparatively rich in purine bases.View full abstractDownload PDF (380K) -
III. Ca2+-Uptake and ATP-SplittingSHINPEI YAMADA, TAIBO YAMAMOTO, YUJI TONOMURA1970 Volume 67 Issue 6 Pages 789-794
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Even in the initial phase of the reaction, 45Ca2+ taken up by the sarcoplasmic reticulum (SR)** was not released on addition of a large amount of EGTA, and was not exchanged with non-radioactive Ca2+.
2. About 2 moles of Ca2+ were taken up by the SR per mole of Ca2+-dependent hydrolysis of ATP under conditions where the release of Ca2+ from the SR was insig-nificant; i.e. in the initial phase of the reaction in the presence of high or low concen-trations of ATP or during all phases of the reaction in the presence of low concen-trations of ATP.
3. All the hydrogen ion released during Ca2+-uptake could be attributed simply to hydrolysis of ATP. Phosphate derived from ATP did not pass through the membrane.View full abstractDownload PDF (336K) -
HIDEYO TAKAHASHI, TOSHIO HIRAI, TAKACHIKA AZUMA, KOZO HAMAGUCHI, SHUNS ...1970 Volume 67 Issue 6 Pages 795-799
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe pH-dependent conformational change of a type K Bence Jones protein (Ta) was studied by circular dichroism (CD)**** and ultraviolet spectroscopy. The conformation of this protein was stable between pH4 and 10 and was changed as the pH was lowered below pH4 or raised above 10. From the total change of the molar extinction coefficient upon acid denaturation it was suggested that two tryptophyl residues of Ta protein are exposed by the denaturation. CD spectra showed that the aciddenatured Ta protein is not randomly coiled but assumes some ordered structure, although the alkali-denatured protein is nearly randomly coiled.View full abstractDownload PDF (282K) -
TAKACHIKA AZUMA, TOSHIO HIRAI, KOZO HAMAGUGHI, SHUNSUKE MIGITA1970 Volume 67 Issue 6 Pages 801-808
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSPotentiometric and spectrophotometric titrations of a type K Bence Jones protein (Ta) were performed at an ionic strength of 0.15, 25°C. It was found that thirty six carboxyl, two α-amino and twenty ε-amino groups have normal pKint values. Two of four imidazole groups have a normal pKint value but the remaining two are masked in the interior of the protein molecule. Only two of the eighteen tyrosyl residues ionize freely without any conformational change. From the change in the electrostatic inter-action factor of the Linderstrom-Lang equation with pH, it was found that a confor-mational change occurs below pH 4.0 and above pH 10.2. This is in good agreement with the results of circular dichroism and ultraviolet absorption spectrum reported in a preceding paper.View full abstractDownload PDF (403K) -
I. Purification, Physical Properties, and Chemical CompositionsSHIGEHARU NAGASAWA, HISAYOSHI SUGIHARA, BYUNG HOON HAN, TOMOJI SUZUKI1970 Volume 67 Issue 6 Pages 809-819
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSBovine plasma α2-macroglobulin was purified from pseudoglobulin fraction by a combination of chromatographies on DEAE-Sephadex A-50 and CM-cellulose, and gel filtrations on Sephadex G-150 and Sepharose 4B. By these procedures, 1.2g of purified preparation could be obtained from two liters of bovine plasma. The purified material was homogeneous as judged by immunoelectrophoresis, starch gel and disc electrophoresis, isoelectric focusing and ultracentrifugation. The α2-macroglobulin was characterized in terms of its major physical and chemical properties. The molecular weight was determined to be approximately 800, 000, and the s02O, W value 17.8 S, the D020, W value 1.93×10-7 cm2/sec, and the_??_value 0.72 were obtained. The isoelectric point of this protein was found to be pH 5.07 indicating that the protein is acidic. The polypeptide portion of α2macroglobulin consisted of 6, 519 amino acid residues and was poor in half-cystine and tryptophan residues. A net negative charge was calculated as 97 from the amino acid analysis and this value was in good accordance with the acidic nature of the protein. The carbohydrate composition was determined to be hexose, 4.50%, glucosamine, 3.l4%, sialic acid, 0.1%, and the molar ratio of mannose to galactose was 1:1. From these results, it was concluded that α2-macroglobulins of human, porcine and bovine plasmas resemble for each other with respect to their physical and chemical properties.View full abstractDownload PDF (2092K) -
II. Interaction of α2-Macroglobulin and TrypsinSHIGEHARU NAGASAWA, BYUNG HOON HAN, HISAYOSHI SUGIHARA, TOMOJI SUZUKI1970 Volume 67 Issue 6 Pages 821-832
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSThe mode of interaction between α2-macroglobulin and trypsin [EC 3. 4. 4. 4] has been investigated with the use of various types of substrates and inhibitors. When trypsin was mixed with α2-macroglobulin, a complex was immediately formed and it was still esterolytically active. The molar binding ratio of trypsin to a, -macroglobulin was deduced to be 3:1. By binding to α2-macroglobulin, hydrolytic activity of trypsin on TAME**** was not affected but hydrolytic activity on TLME decreased to 65%. From kinetic analyses, it was found that maximum velocities (Vmax) of hydrolysis of BAEE and BAPNA by trypsin were decreased to 23% and 52%, respectively, by α2-macroglobulin. α2-Macroglobulin strongly inhibited the proteolytic activity of trypsin. Caseinolytic and fibrinogenolytic activities were observed to be decreased by 91% and 100%, respectively.
Esterolytic activity of the α2-macroglobulin-trypsin complex was not blocked by protein inhibitors, such as SBTI, EWTI or LBTI, but was blocked by the low molecular weight polypeptide inhibitor, Trasylol, or active site specific inhibitors, such as TLCK and DFP. These results suggested that no part of the active site region in trypsin was implicated in the binding to α2macroglobulin.
From these results, a possible mode of interaction between α2-macroglobulin and trypsin was presented as follows; in the α2-macroglobulin-trypsin complex the catalytic site lies in a crevice. Low molecular weight synthetic substrates or inhibitors can diffuse into the crevice, whereas bulkier protein substrates or inhibitors can not.
Acid treatment of the α2-macroglobulin-trypsin complex at pH 2.0 restores the accessibility of the catalytic site to protein substrate as well as protein inhibitors. By the acid treatment, about 40% of the total amount of trypsin was dissociated from the complex.
Since it was observed that the α2-macroglobulin-trypsin complex dissociates in acidic solution and that trypsin binding activity of α2-macroglobulin was decreased by treatment with methylamine, it was supposed that carboxylate groups in α2-macroglobulin might be implicated in the binding of trypsin.View full abstractDownload PDF (780K) -
IX. Photooxidation of Ribonuclease T1 in the Presence of Rose BengalKENJI TAKAHASHI1970 Volume 67 Issue 6 Pages 833-839
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESS1. Ribonuclease T, [EC 2. 7. 7. 26] was rapidly inactivated by rose bengal-catalyzed photooxidation at pH 8.5 and 37°C, losing the activity toward both RNA and 2', 3'-cyclic guanylate in parallel. The activity was lost more slowly at pH 7.0 and little inactivation occurred at pH 5.5, suggesting the implication of histidine residues in the inactivation.
2. The only marked changes occurred with histidine and tryptophan residues. About 70% and over 90% inactivation, respectively, took place when one and two histidine residues per molecule of protein were lost. The tryptophan residue was lost much more slowly; the loss was only 0.2 residue per molecule of protein at the level of 80%o inactivation. The reactivity of the γ-carboxyl group of the active site glutamic acid-58 toward iodoacetate was also diminished markedly.
3. These results thus show clearly that the photooxidation of one or two histidine residues are directly responsible for the inactivation, and hence that one or both of them are involved in the active center of the enzyme.View full abstractDownload PDF (369K) -
KUNIHIKO SAITO, MASAMI GAMO1970 Volume 67 Issue 6 Pages 841-849
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSEvidence is presented here for the first time that diol waxes in the preen gland of the green pheasant were composed mainly of diesters of 2, 3-dihydroxyoctadecane. The structures of such long chain diols were determined as follows: the samples were converted to corresponding hydrocarbons through p-toluenesulfonyl derivatives and preparation of isopropylidene derivatives and periodate oxidation were carried out. The reaction products were analyzed by gas chromatography or by combined gas chromatog-raphy-mass spectrometry. The constituent fatty acids were determined to be lauric, n-tridecanoic, myristic, n-pentadecanoic, palmitic, n-heptadecanoic and stearic acids. Dint waxes of the domestic hen, on the other hand, were reconfirmed to consist of diesters of 2, 3-dihydroxy-docosane, -tricosane and -tetracosane in addition to several minor homologues.View full abstractDownload PDF (1080K) -
KEIKO MATSUZAKI1970 Volume 67 Issue 6 Pages 851-855
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (225K) -
HISASHI MIYAZAKI, TADAHIKO KARASAWA, YASUO MINAKI, YOSHIO YOSHIMURA1970 Volume 67 Issue 6 Pages 857-858
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (115K) -
NORIO HAYASHI, BINKOH YODA, GORO KIKUCHI1970 Volume 67 Issue 6 Pages 859-861
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (157K) -
YASUO KURASHIMA, NORIO HAYASHI, GORO KIKUCHI1970 Volume 67 Issue 6 Pages 863-865
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (160K) -
DAISUKE TSURU, TOMOCIKA YOSHIDA, JUICHIRO FUKUMOTO1970 Volume 67 Issue 6 Pages 867-869
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (173K) -
JUNZO KATO, YACHIYO ATSUMI, MASAMI MURAMATSU1970 Volume 67 Issue 6 Pages 871-872
Published: June 25, 1970
Released on J-STAGE: November 18, 2008
JOURNAL FREE ACCESSDownload PDF (141K)
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