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Volume 24 (1980 - 198･･･
- Issue 4 Pages 289-
- Issue 3 Pages 203-
- Issue 2 Pages 115-
- Issue 1 Pages 19-
Volume 24, Issue 2
Displaying 1-8 of 8 articles from this issue
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Hidematsu Hirai1980 Volume 24 Issue 2 Pages 115-120
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
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H. G. Schwick1980 Volume 24 Issue 2 Pages 121-148
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
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Mary Osborn1980 Volume 24 Issue 2 Pages 149-170
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
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2. Isolation of J-chain and its immunological and physicochemical propertiesKunihiko Kobayashi, Hidematsu Hirai1980 Volume 24 Issue 2 Pages 171-176
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA homologue of J-chain was purified from chicken serum IgM by ion-exchange chromatography on DEAE-cellulose followed by gel-filtration. Purified chicken J-chain showed a similar molecular weight to human J-chain and its molecular weight was calculated to be 19, 000 daltons.
The amino acid composition of chicken J-chain was also determined and a striking similarity in the content of systeine was found between J-chain of chicken and mammals. However, marked differences in amino acid composition of chicken J-chain were also observed in the contents of glutamic acid, asparatic acid, isoleucine, glycine, leucine and phenylalanine, when compared with those of mammalian J-chains. In spite of such differences in amino acid composition between J-chain of chickens and mammals, a precipitative cross-reaction between J-chain of chickens and human was observed with the antiserum to human J-chain, when reaction was proceeded in agarose gel incorporated with polyethylene glycol (Precipiplex).
NH2-terminal amino acid could not be detected in the dansylated J-chain, possibly indicating the blocked terminus similar to the human counterpart.
A component which was different from the J-chain in respects of its antigenicity and molecular weight (30, 000 daltons) but which had an electrophoretic mobility similar to J-chain on alkaline-urea-PAGE was identified in the chicken IgM. It was associated with the IgM by disulfide linkage and could possibly be confused with the chicken J-chain.View full abstractDownload PDF (7249K) -
Masato Ageta, Seiichiro Yamazaki, Hisatoshi Bekki, Toshinori Akiyoshi, ...1980 Volume 24 Issue 2 Pages 177-182
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSEighty-seven patients were divided into two groups such as coronary heart disease (CHD) and non-CHD by the method of coronary angiography. High density lipoprotein-cholesterol (HDL-TCh), very low density lipoprotein total cholesterol/trigryceride (VLDL-TCh/TG) and β-K band were measured in all of the patients after the experimental diet treatment. HDL-TCh in the CHD was significantly lower than that in the non-CHD group, P<0.001. There were, however, no correlation between HDL-cholesterol concentration and the location of coronary arterial stenosis. HDL-TCh and VLDL-TCh/TG were related with the grade of coronary arterial irregularity. An increased grade of the irregularity was accompanied with the lower concentration of HDL-TCh, and the higher ratio of VLDL-TCh/TG. A frequency of the β-K band was significantly higher in the CHD (45.9%) as compared with that in the non-CHD (12.1%). Particularly, twenty-two patients with the irregural coronary artery were showed 68.1%, whereas the patients without the irregularity were only 13.3%. A negative relation between HDL-TCh and VLDL-TG was found in the non-CHD, whereas the CHD was r=0.444.
These results might be of interest in the view of HDL-cholesterol as a well documented and dependent “irregularity of coronary artery.” And this is based on a lipoprotein metabolism correlating between HDL and VLDL fraction. In this investigation a clinical significance of HDL-cholesterol for coronary heart disease has been studied. Particularly, a relationship between the conformation of coronary artery and HDL-TCh was discussed.View full abstractDownload PDF (3549K) -
Joji Hori1980 Volume 24 Issue 2 Pages 183-186
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe alkaline denaturation of bovine serum albumin was studied by acrylamide gel electrophoresis at pH 9.0. The gel patterns were similar to those for the alkali-denatured human serum albumin, and it is concluded that there were also the “first and second reactions.” The intrinsic viscosity of the alkali-denatured bovine serum albumin was determined at pH 9.0 and 20°C. Data obtained support this conclusion.View full abstractDownload PDF (2816K) -
Tsuneyoshi Horigome, Kaoru Yoshida, Yuko Kanai, Kazuko Hasegawa, Hiros ...1980 Volume 24 Issue 2 Pages 187-190
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSAn improved method for the analysis of low molecular weight polypeptides (<molecular weight 10, 000) by SDS-polyacrylamide gel electrophoresis was described. Linear gradient polyacrylamide gels, 10-20% [1:20(w/w) bisacrylamide: acrylamide], with a stacking gel gave good resolution. Separation gels also contained 0.45M Tris-HCl (pH 8.8), 0.1% SDS and 7M urea, as well as a 0-10% linear gradient of sucrose. Polypeptides having molecular weights from 1, 400 to 100, 000 could be analyzed by this gel system. Moreover, leakage of low molecular weight polypeptides from gels in the staining procedure had been lowered by using the relatively high concentration of bisacrylmaide. This method could be applied for the analysis and detection of low molecular weight polypeptides from complex biological sources.View full abstractDownload PDF (4365K) -
A Mathematical ApproachKazuo Shimao1980 Volume 24 Issue 2 Pages 191-194
Published: September 25, 1980
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSDownload PDF (247K)
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