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Volume 33 (1989)
- Issue 6 Pages 273-
- Issue 5 Pages 216-
- Issue 4 Pages 155-
- Issue 3 Pages 113-
- Issue 2 Pages 67-
- Issue 1 Pages 17-
Volume 33, Issue 6
Displaying 1-7 of 7 articles from this issue
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Tatehiko Tanaka1989 Volume 33 Issue 6 Pages 273-278
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA new technique, ligand saturating affinity electrophoresis, was developed for determining the concentration of anti-dextran IgG in rabbit serum. In the presence of an excess of intermediary molecular size dextran in the polyacrylamide gel, polyclonal anti-dextran IgG migrated in a single sharp band, separated from the nonspecific IgG fraction and other serum protein fractions. With this technique, 1-10μg anti-dextran IgG in antiserum can be determined within 3h.View full abstractDownload PDF (4603K) -
A method of direct detection on cellulose acetate membrane after isoelectric focusingMasafumi Kamada, Yoshiko Someya, Masahiko Ikekita, Kazumasa Aoki, Kazu ...1989 Volume 33 Issue 6 Pages 279-283
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSIn this report, a new convenient method for detecting (micro-) heterogeneous components of tissue kallikrein with high sensitivity has been demonstrated. This method consists of an isoelectric focusing on cellulose acetate membrane and a direct immunodetection of kallikrein bands on cellulose acetate membrane using anti-tissue kallikrein anti-rabbit serum without any blotting technics. This method is specific for tissue kallikrein and has a high sensitivity for detecting (micro-) heterogeneous components at below 10ng of each one. This method also can detect (micro-) heterogeneous components of tissue prokallikrein, because anti-tissue kallikrein rabbit serum can react with tissue prokallikrein.View full abstractDownload PDF (3953K) -
Kazuhisa Taketa, Masao Fukunaga, Rikushi Morita, Yoshiatsu Kanbara, Hi ...1989 Volume 33 Issue 6 Pages 285-291
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSActivities of alkaline phosphatase isozyme 3 (ALP3) in healthy adults (27 males and 36 females), ranging in age from 24 to 67 years old with a mean and standard deviation of 45.3±9.4, were estimated from the total activities of ALP and the fractions of ALP3 among ALP isozymes separated by electrophoresis on cellulose acetate membranes. When mean values among different blood groups were compared, the ALP3 activity and age in blood group B were higher than those in blood group AB, and the osteocalcin level in blood group B was highest. ALP3 activities in male and female groups were not different. In females, ALP3 activity correlated positively with the level of osteocalcin, but not with that of parathyroid hormone (PTH), although the total ALP activity correlated with both osteocalcin and PTH. Age correlated with both ALP3 and PTH, but not with osteocalcin. The wide distribution of ALP3 activity observed in the healthy adults, ranging from 44 to 168IU/l with a mean and standard deviation of 89.3±28.4, could be explained by the modulation of osteoblastic activity and indirectly by the age-dependent alteration of parathyroid status in female subjects.View full abstractDownload PDF (2338K) -
Kazuyuki Nakamura, Tatehiko Tanaka, Kazusuke Takeo1989 Volume 33 Issue 6 Pages 293-303
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSProteins bound to a nitrocellulose (NC) membrane tightly and quantitatively until the NC membrane was saturated with the proteins. The binding of proteins to the NC membrane was characterized by using twenty proteins having different molecular weight and isoelectric point as follows: 1) hydrophobic interactions between the protein and the NC membrane matrices may play a major role in the protein binding, and sugars, amino acids, DNA, nucleotides, neutral salts, or glycerol in the protein solution did not interfere with the protein binding. 2) The number of the protein molecule bound to the NC membrane was in the range from 1.13 to 1.98nmol/cm2 except for a few small and strongly charged proteins. 3) Non-ionic detergents such as Tween 20, Triton X-100, and Nonidet P-40 strongly interfered with the protein binding to the NC membrane in a concentration dependent manner. 4) Proteins could be extracted from the NC membrane with high yield by using a low concentration of the non-ionic detergent. These enables us to assay the proteins with high sensitivity and reproducibility. Furthermore, it may be possible to determine the amino acid composition and sequence with small amount of the proteins after the assay.View full abstractDownload PDF (1248K) -
Kazuyuki Nakamura, Tatehiko Tanaka, Kazusuke Takeo1989 Volume 33 Issue 6 Pages 305-312
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA technique of chromatography using a nitrocellulose (NC) membrane was established for the separation of proteins. The proteins were developed on the NC membrane with an aqueous solution containing a non-ionic detergent, polyoxyethylene sorbitane (Tween 20). The rate of flow of the proteins correlated to the strength of hydrophobicity of the proteins which was theoretically calculated from the hydrophobicity of side chains of amino acid residues composed of the proteins, but neither to the molecular weight nor to the isoelectric point of the proteins. The detailed examinations on the effects of pH, temperature, and chemicals such as urea, neutral salts, methanol, and an ionic detergent (SDS) on the chromatography strongly suggested that hydrophobic interactions between the proteins and nitrocellulose play a major role in the protein binding to nitrocellulose membrane. So that, this technique may be useful for the separation of a very small amount of membrane bound proteins such as enzyme complexes, receptors, and ribosomes into their components.View full abstractDownload PDF (7268K) -
Takanori Moriyama, Manabu Nobuoka, Yuichi Takasugi, Mikio Makino1989 Volume 33 Issue 6 Pages 313-317
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe biochemical properties of macro creatine kinase type 1 found in seven patients and type 2 found in one case were examined. In the cases of macro creatine kinase type 1, three patients with creatine kinase BB linked immunoglobulin G and three patients with creatine kinase MM linked immunoglobulin A were determined. Two forms of macro creatine kinase were easily differentiated by the determination of their distinct activation energies. Molecular masses of macro creatine kinase type 1 were approximately estimated to be from 230, 000 to 330, 000, and multi-molecular forms of macro creatine kinase type 2 were observed by the method of gel permeation high performance liguid chromatography. Two forms of macro creatine kinase were mainly detected in patients with malignancies.View full abstractDownload PDF (533K) -
Midori Wada, Kiyoko Shiba, Akihiko Shiba1989 Volume 33 Issue 6 Pages 319-325
Published: December 15, 1989
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe analysis of gingival fluid proteins was performed by the combinative method of microscale two-dimensional electrophoresis with the highly sensitive silvers taining, which was possible to measure a minute amount of sample. 31-55 protein spots were detected, and 14 proteins of them were identified by electroblotting-immunochemical staining. As compared gingival fluid with mixed saliva and serum, the spots of isoelectric point of pI 5.2-5.5 and MW 130, 000-140, 000 were characteristic of gingival fluid. In the quantitative comparison, the IgA, ceruloplasmin and α2-HS glycoprotein spots were more deeply stained on the serum, while IgG and albumin spots were more deeply stained on the gingival fluid. We also demonstrated the presence of a haptoglobin with different pI position in gingival fluid, and recognized that the haptoglobin-hemoglobin complex observed in alkaline side were present in the advanced inflammatory conditions. We would like to conclude that a complex of haptoglobin and hemoglobin is closely related to inflammatory responses.View full abstractDownload PDF (7282K)
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