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Volume 35 (1991)
- Issue 6 Pages 417-
- Issue 5 Pages 339-
- Issue 4 Pages 253-
- Issue 3 Pages 155-
- Issue 2 Pages 59-
- Issue 1 Pages 1-
Volume 35, Issue 2
Displaying 1-11 of 11 articles from this issue
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1991 Volume 35 Issue 2 Pages 59-60
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
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1991 Volume 35 Issue 2 Pages 61-66
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
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1991 Volume 35 Issue 2 Pages 67-87
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
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1991 Volume 35 Issue 2 Pages 88-97
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
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Haruhiro Yoshida, Shigenori Ikemoto1991 Volume 35 Issue 2 Pages 99-105
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSFor the purpose of the paper was to search for markers for individual identification of human seminal plasma samples by micro two-dimensional polyacrylamide gel electrophoresis (M2D-PAGE) and capillary isotachophoresis (CITP). The coomassie-stained M2D-PAGE patterns of seminal plasma protein showed the individual difference in the spots of Acp, Alb, Tf and γ-Sm. The individual differences in UV absorbance peaks in CITP patterns were correlated with those spots in M2D-PAGE patterns. Thirteen spots were detected in the zone of lower molecular weight around 5, 000 by silver staining after M2D-PAGE in the gradient of 6 to 25% for the second dimensional development. Three of the spots named low molecular weight seminal plasma protein showed the individual difference, Six phenotypes were detected in the human seminal plasma.View full abstractDownload PDF (7454K) -
Motoo Matsuda, Kazumasa Matsumoto, Choji Kaneuchi, Toshio Masaoka, Fum ...1991 Volume 35 Issue 2 Pages 107-112
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSIn order to determine the suitable conditions for gaining distribution of DNA fragments useful for the chromosomal DNA analysis of the thermophilic Campylobacter, C. coli, C. jejuni and C. laridis, we were interested in the poor G+C content of the chromosomal DNAs and the intact DNAs embedded in agarose blocks were digested with 15 restriction enzymes which can recognize sequences containing only G and C nucleotides (NotI, SfiI, ApaI, BglI, SacII, SmaI and HpaII), sequences rich with G and C (BamHI, KpnI, PstI, SalI and XhoI) and some other sequences (DraI, EcoRI and HindIII) respectively. The resulted restriction fragments were fractionated by pulsed-field gel electrophoresis.
When the chromosomal DNAs prepared from the 3 Campylobacter strains were digested with two restriction enzymes (NotI and SfiI) available with 8-base recognition, electrophoretic profiles of the digested chromosomal DNAs were shown to be very similar to those of each undigested chromosomal DNAs, respectively.
The DNAs digested with EcoRI migrated at the same level as each undigested chromosomal DNAs by unknown reason(s).
Twelve other restriction enzymes were able to cut the DNAs from the 3 Campylobacter strains with the exception that KpnI did not cut the DNA from the C. jejuni strain. Among the enzymes, ApaI, SalI and SmaI cut the DNAs from the 3 Campylobacter strains into a relatively limited number of restriction fragments in the range of approximately 50-1, 500kb in length.
Thus, three restriction enzymes, ApaI, SalI and SmaI, were found to produce distributions of DNA fragments useful for chromosomal DNA analysis of the 3 Campylobacter strains by pulsed-field gel electrophoresis.
Moreover, the genome size of the 3 bacterial strains were preliminarily estimated to be approximately 2, 000kb for C. coli JCM 2529T, 1, 900kb for C. jejuni JCM 2013 and 1, 700kb for C. laridis JCM 2530T in length, respectively.View full abstractDownload PDF (4050K) -
Shiro Kashiwagi, Kazuyuki Nakamura, Kazusuke Takeo, Haruhide Ito1991 Volume 35 Issue 2 Pages 113-120
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe interaction between plasma fibronectin and gelatin was analysed by affinity electrophoresis, and effects of pH, urea, 2-mercaptoethanol and temperature on the interaction were examined. The fibronectin was electrophoresed with 4% polyacrylamide gel in the absence and presence of gelatin and the fibronectin band was stained by immunoblotting. Dissociation constants (Kd) of fibronectin for gelatin were calculated from the affinity plot based on the original affinity equation (Takeo, K.: Electrophoresis, 5: 187, 1984) at different pHs. The fibronectin had higher affinity to gelatin at pH9.5 than pH3.8. The affinity decreased in the presence of urea. KdS at 37°C were 1.49×10-7M, 2.50×10-6M and 3.58×10-6M with 2M, 3M and 4M urea, respectively. The fibronectin decreased its affinity in a stepwise fashion at the increase in concentration of 2-mercaptoethanol. This suggested that conformational changes of the fibronectin occur due to the stepwise reduction of inter- and intrachain disulfide bonds. The van't Hoff analysis of the temperature dependence of Kd values showed that relationship of log Kd and 1/T was inversely proportional in the temperature range between 15°C and 50°C. The affinity was not detected at 60°C. These data suggested that the hydrogen bond and van der Waals' interaction play important role for the binding of plasma fibronectin to gelatin.View full abstractDownload PDF (5207K) -
Manabu Yamamoto1991 Volume 35 Issue 2 Pages 121-128
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA method of sodium dodecyl sulfate poly-acrylamide gel electrophoresis (SDS-PAGE) followed by immuno-blotting has been established for measurement of type II collagen in samples contaminated with type I collagen.
Using SDS-PAGE, the content of type II collagen within the range from 0.13μg to 0.51μg could be determined using the samples in which the type II collagen was mixed with type I collagen less than 0.24μg.
Using immuno-blotting method, it was possible to detect 1.5ng of type II collagen and to measure the content of type II collagen in the range from 3ng to 75ng.View full abstractDownload PDF (2950K) -
Iron incorporation and ferroxidase activityKeiko Yamaguchi, Shinichirou Iida, Yasunori Aoki, Takashi Katayama, Hi ...1991 Volume 35 Issue 2 Pages 129-133
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSIn this study iron incorporation and ferroxidase activity of 3'-Me-DAB hepatoma ferritin (RHpF) were investigated and compared with those of normal liver and heart ferritins (RLF, RHF). Isoelectrophoretic pattern of RHpF shifted to acidic side and the proportion of H subunit increased as compared with RLF. However, the rate of iron incorporation and ferroxidase activity of RHpF were lower than those of RLF. On the other hand, RHF, H rich ferritin showed the highest rate and activity of the tested ferritins. From these results it is speculated that the property of H subunit of hepatoma ferritin may be different from that of normal ferritins.View full abstractDownload PDF (549K) -
Hiroaki Minami, Osamu Yahara, Sokichi Onodera1991 Volume 35 Issue 2 Pages 135-141
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe quantitative changes in the structural proteins of myocardial hypertrophy have not been known well.
We modified the quantitative method of the structural protein using the two-dimensional electrophoresis and the pyridine extraction, and analyzed the changes of myocardium.
As experimental animal, we used three models of left ventricular hypertension consisted of spontaneously hypertensive rats, aortic-constricted rats and two-kidney one clip hypertensive rats.
It was usually difficult to analyze high molecular proteins according to the first dimension electrophoresis, so that we used agarose instead of polyacrylamide in the first dimension and homogenized cardiac muscle with 8M guanidine hydrochloride without the degradation of proteins.
Because of the simultaneous determination of the major and minor components on a slab gel, we analyzed the coloring extracts from spots stained by 25% pyridine.View full abstractDownload PDF (1695K) -
Mami Miyachi, Kaori Sakurai, Minoru Tozuka, Tetsurou Ichikawa, Tsutomu ...1991 Volume 35 Issue 2 Pages 143-149
Published: April 15, 1991
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSWe found a lactate dehydrogenase-immunoglobulin G (LDH-IgG) complex with abnormally low serum LDH activity (43U/l) in a patient removed partially his tongue with carcinoma. The LDH isoenzyme pattern of the patient's serum was composed of three abnormal bands only adjacent to the position of LDH4. When the LDH activity gradually increased, the LDH isoenzyme pattern changed to another abnormal pattern containing five bands at the positions of LDH1-5 and other extra bands. As the results of a recombination study between LDH and IgG linked LDH, it was paralleled the sequential change of the patient's LDH activity and transition of LDH isoenzyme pattern caused by their molecular ratio. Inhibition rate of LDH activity by IgG linked LDH was not altered at 0°C and room temperature, and no significant change was observed after 24h at both temperature.View full abstractDownload PDF (5659K)
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