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Volume 30, Issue 1
Displaying 1-10 of 10 articles from this issue
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Toshiaki Isobe, Tsuneo Okuyama1986 Volume 30 Issue 1 Pages 19-26
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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Mei Satake1986 Volume 30 Issue 1 Pages 27
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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Itaru Toyoshima1986 Volume 30 Issue 1 Pages 29-35
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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Tomoko Tashiro1986 Volume 30 Issue 1 Pages 37-44
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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Keiichi Uyemura, Kunio Kitamura, Masaru Suzuki, Yasushi Sakamoto, Kazu ...1986 Volume 30 Issue 1 Pages 45-51
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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Yasuo Takahashi, Toru Yamakuni1986 Volume 30 Issue 1 Pages 53-58
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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Toshiho Nishita1986 Volume 30 Issue 1 Pages 59-65
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSPeptide maps prepared by trypsin digestion of equine CA-III disclosed the presence of 26 peptides. Amino acid analysis of the eluates of each peptide spot indicated there were 12 peptides that contained arginine, 13 peptides that contained lysine and one peptide that contained both arginine and lysine. A map prepared by trypsin digestion of citraconylated CA-III disclosed the presence of 13 peptides. Amino acid analysis of each peptide identified 8 peptides containing arginine, one peptide containing lysine and four peptides containing both lysine and arginine. The peptide map of CA-IIIa corresponded to that of CA-III except for the absence of peptide No. 25. The amino acid composition of each peptide from equine CA-III was compared to the sequence of bovine CA-III in order to establish a model of the equine CA-III sequence. It was estimated that the homology of the sequence between equine CA-III and bovine CA-III is high.View full abstractDownload PDF (636K) -
Masato Ageta, Takaharu Taniguchi, Fumimasa Ishii, Shinji Uchiyama, Hik ...1986 Volume 30 Issue 1 Pages 67-73
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESS2-mercaptopropionyl-gylcine (2-MPG) is one of the agents having a protective action against lipid peroxidation in vitro. Human low density lipoprotein (LDL) was easily denatured by an interaction with linoleic acid hydroperoxide or 85% of oxygen in our previous studies. The purpose of this study was to determine effects of 2-MPG on the formation process of denatured LDL which was due to interaction with linoleic acid hydroperoxide or 85% of oxygen. Human LDL was isolated from 6 healthy volunteers after an over-night fast. The isolated LDL was treated with 2-MPG, before an incubation with linoleic acid hydroperoxide or a saturation with 85% O2. Lipid staining pattern of the isolated LDL on polyacrylamide gel disc electrophoresis was modified by the interaction with linoleic acid hydroperoxide, and the incidence of modified LDL was dependent on time of the interaction and dose of the hydroperoxide at 37°C. The incidence was significantly reduced by the treatment with 2-MPG. Moreover, the effect of 2-MPG was dose-dependent. Lipid peroxide concentration in the isolated LDL was markedly increased under the condition saturated with 85% O2, whereas one in the pre-treated LDL with 2-MPG was not increased. The increase in LDL-lipid peroxide concentration was negatively correlated with the dose of 2-MPG. The results suggest that 2-MPG can prevent the formation of denatured human LDL. It is possible that the effect of 2-MPG is brought about by the inhibition of lipid peroxidation in lipoprotein particle.View full abstractDownload PDF (745K) -
Hirokazu Usuda, Masatoshi Fujishiro, Tsutomu Inoue1986 Volume 30 Issue 1 Pages 75-82
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe protein constituents of albumen gland from Euhadra subnimbosa, E. peliomphala, and E. p. simodae were analyzed by SDS polyacrylamide gel electrophoresis. Furthermore, peptide maps of three species were studied by two-dimensional electrophoresis with high sensitive silver stain and standardized. A unique peptide map was obtaind from albumen gland of each species. The peptide maps of E. peliomphala and E.p. simodae were especialy similar.
Effect of the steroid hormone, 17β-estradiol, on protein synthesis of albumen gland (E. subnimbosa in hibernation) was analyzed by O'Farrell's 2-dimensional electrophoresis. Five peptide groups in peptide map, (No.5, 8, 9, 11, and 13), were commonly found in some individuals of 17β-estradiol injected snails. These five peptide groups were detected to a normal individual in feeding.
We suggested that the five peptide groups, (No.5, 8, 9, 11, and 13), inducibled by 17β-estradiol.View full abstractDownload PDF (8145K) -
Sumiko Hashimoto, Kinya Kawano1986 Volume 30 Issue 1 Pages 83-84
Published: February 28, 1986
Released on J-STAGE: March 31, 2009
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