-
Shozo YAMAMOTO, Tanihiro YOSHIMOTO, Natsuo UEDA, Chieko YOKOYAMA
Article type: Article
1988 Volume 62 Issue 1 Pages
1-13
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
Monoclonal antibodies were raised against arachidonate 12- and 5-lipoxy-genases of porcine leukocytes using partially purified enzyme as antigen. The two lipoxygenases were highly purified by immunoaffinity chromatography utilizing the anti-lipoxygenase antibodies. Studies with the purified enzymes demonstrated their multi-functional catalytic properties. In addition to 12-oxygenation of arachidonic acid, the purified 12-lipoxygenase catalyzed 8S- and 14R-oxy-genation and 14,15-epoxidation of 15-hydroperoxyeicosatetraenoic acid. 5-Lipoxygenase showed both arachidonate 5-oxygenation and 5,6-epoxidation of 5-hydroperoxy acid (leukotriene A_4 Synthesis). Lipoxin synthesis from 5,15-dihydroperoxy acid was demonstrated with both 12- and 5-lipoxygenases.
View full abstract
-
Toshiyuki NAKATSUKA, Kiroku SUZUKI, Yoshihisa NAKANO, Shozaburo KITAOK ...
Article type: Article
1988 Volume 62 Issue 1 Pages
15-22
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
In the preceeding paper, purification procedure and some enzymatic properties of thiaminase 11 produced intracellularly from Bacillus aneurinolyticus were reported. In this paper the physicochemical properties of the enzyme was de-scribed. Thiaminase 11 had a molecular weight of 180,000 determined by gel filtration. The physicochemical values of the enzyme protein were 5.88 (S^0_<20.w.>), 0.792 cm^3/g (sp. vol.), 2.89×10^<-7>cm/sec of (diffusion const.) and 182,000 (mol. wt.) calculated from these constants supporting the result of gel filtration. The enzyme consisted of 10 homogeneous polypeptides and the subunit was composed of 175 amino acids including three SH groups. The enzyme contained one mole of glucosamine per subunit and some sugars, indicating that the enzyme is a glycoprotein. The amino-terminal amino acid was Met and carboxy-terminal Ser. Isoelectric point of the enzyme was 4.55.
View full abstract
-
Shoji YAMADA, Shoki TERADA, Kenichiro HIRATA, Kainosuke SAITO, Morimic ...
Article type: Article
1988 Volume 62 Issue 1 Pages
23-30
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
A hog intestinal receptor for intrinsic factor-vitamin B_<12> complex was purified by combined affinity chromatography, gel filtration and isoelectric focusing. The final product had the specific activity of 2,480pg vitamin B_<12> binding through intrinsic factor/mg protein and the recovery was 62.5%. Sodium dodecylsulfate polyacrylamide gel electrophoresis showed main protein bands corresponding to molecular weight of 470,000 and 222,000 in the absence or presence of a reducing agent respectively. Rabbit anti-serum which had been produced against the purified receptor preparation bound receptor-intrinsic factor-vitamin B_<12> to form a macromolecular complex. Fluorescein antibody technique by the sandwich method using the anti-serum showed that the receptor was localized both in the proximal and distal portion of the intestine but neither in the stomach nor in the liver.
View full abstract
-
Shoji YAMADA, Morimichi FUKUDA, Kainosuke SAITO, Shoki TERADA, Kenichi ...
Article type: Article
1988 Volume 62 Issue 1 Pages
31-36
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
A purified hog intestinal receptor for intrinsic factor-vitamin B_<12> complex was labeled with ^<125>I. The labeled receptor had an apparent molecular weight of 460,000 on gel filtration through Sepharose 6B column and an isoelectric point of 4.48. It reacted with the anti-serum against the receptor to yield a macromolecular complex. When the receptor was assayed in a double anti-body radioimmunoassay using the ^<125>I-labeled receptor, good standard curves were obtained and non-specific, binding was less than 1.2%. A good agreement was obtained between receptor activities assayed by gel filtration and receptor contents measured by the present radioimmunoassay method by studying several receptor preparations with different specific activities. The method is simple to perform, precise and sensitive and makes it possible to assay the receptor in large batches.
View full abstract
-
[in Japanese], [in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
37-38
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
38-39
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...
Article type: Article
1988 Volume 62 Issue 1 Pages
39-40
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
40-41
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
41-42
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
42-
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese], [in Japanese], [in Japanese], [in Japane ...
Article type: Article
1988 Volume 62 Issue 1 Pages
42-43
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
43-44
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
44-
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
45-47
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
47-48
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
48-49
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese], [in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
49-50
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS
-
[in Japanese]
Article type: Article
1988 Volume 62 Issue 1 Pages
51-
Published: January 25, 1988
Released on J-STAGE: March 16, 2018
JOURNAL
FREE ACCESS