Pub Date : 1995-06-30DOI: 10.14921/JSCC1971B.24.2_74
K. Shishino, S. Saheki, N. Takeuchi
{"title":"Glycated Apo B Protein and Vascular Complications in Diabetes Mellitus","authors":"K. Shishino, S. Saheki, N. Takeuchi","doi":"10.14921/JSCC1971B.24.2_74","DOIUrl":"https://doi.org/10.14921/JSCC1971B.24.2_74","url":null,"abstract":"","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1995-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735348","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1995-03-31DOI: 10.14921/JSCC1971B.24.1_32
T. Higashino, Kunio Kobayashi, K. Hirauchi, K. Uchida
An immunological pretreatment method using a microplate was developed for fractional determination of low concentrations of a-fetoprotein (AFP) in serum. This method allows simultaneous partial purification and concentration of AFP from many serum samples. The pretreated sample can then be subjected to lectin-affinity electrophoresis (LAE) coupled with detection by antibody-affinity blotting. More than 60% of the AFP was recovered by the partial purification from serum containing less than 100 pg/I of AFP, and the specific activities for the total protein was raised more than 20-fold. There was no bias or shift in AFP composition between the untreated and partially purified samples. By the present pretreatment method, AFP at a concentration of as low as 10 pg/I in serum was concentrated and detected by the LAE coupled with the antibody-affinity blotting.
{"title":"Pretreatment of Serum Using a Microplate for Fractional Determination of Low Concentrations of α-Fetoprotein","authors":"T. Higashino, Kunio Kobayashi, K. Hirauchi, K. Uchida","doi":"10.14921/JSCC1971B.24.1_32","DOIUrl":"https://doi.org/10.14921/JSCC1971B.24.1_32","url":null,"abstract":"An immunological pretreatment method using a microplate was developed for fractional determination of low concentrations of a-fetoprotein (AFP) in serum. This method allows simultaneous partial purification and concentration of AFP from many serum samples. The pretreated sample can then be subjected to lectin-affinity electrophoresis (LAE) coupled with detection by antibody-affinity blotting. More than 60% of the AFP was recovered by the partial purification from serum containing less than 100 pg/I of AFP, and the specific activities for the total protein was raised more than 20-fold. There was no bias or shift in AFP composition between the untreated and partially purified samples. By the present pretreatment method, AFP at a concentration of as low as 10 pg/I in serum was concentrated and detected by the LAE coupled with the antibody-affinity blotting.","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1995-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735339","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1995-03-31DOI: 10.14921/JSCC1971B.24.1_25
N. Okumura, F. Terasawa, M. Tozuka, T. Katsuyama, K. Furihata
{"title":"Comparison and Evaluation of Three FDP Values Determined by an Automated Latex Photometric Immunoassay System Using Anti-Fibrinogen, Anti-Fibrinogen-E Domain, or Anti-Neoantigen of Fibrinogen-D Domain Antibody","authors":"N. Okumura, F. Terasawa, M. Tozuka, T. Katsuyama, K. Furihata","doi":"10.14921/JSCC1971B.24.1_25","DOIUrl":"https://doi.org/10.14921/JSCC1971B.24.1_25","url":null,"abstract":"","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1995-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735289","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1995-01-01DOI: 10.14921/JSCC1971B.24.3_146
S. Nakagawa, Masahiko Munechika
{"title":"A Study on an Analysis System for Quality Control Surveys","authors":"S. Nakagawa, Masahiko Munechika","doi":"10.14921/JSCC1971B.24.3_146","DOIUrl":"https://doi.org/10.14921/JSCC1971B.24.3_146","url":null,"abstract":"","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1995-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66734902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1994-12-31DOI: 10.14921/JSCC1971B.23.4_299
T. Ikegami, Masatoshi Yamamoto, Yoshihiro Sato, Masaharu Takahashi, S. Usuda, M. Maeda, A. Tsuji
We developed an anti-GOR assay using the LuminomasterTM system, a fully automated, random access chemiluminescent enzyme immunoassay system. GOR antibody, which is often detected in the serum of patients infected withHepatitis C virus (HCV), is closely associated with HCV infection. This new assay provides detection of GOR antibody in 45 min, about half the time of existing EIA methods. The standard curve is 0.1-300 GOR unit/ml (1/10th-300 times cut-off value), giving a detection range about 30 times greater than that of existing assays. This greater detection
{"title":"Development of a Fully Automated Chemiluminescent Enzyme Immunoassay for GOR Antibody","authors":"T. Ikegami, Masatoshi Yamamoto, Yoshihiro Sato, Masaharu Takahashi, S. Usuda, M. Maeda, A. Tsuji","doi":"10.14921/JSCC1971B.23.4_299","DOIUrl":"https://doi.org/10.14921/JSCC1971B.23.4_299","url":null,"abstract":"We developed an anti-GOR assay using the LuminomasterTM system, a fully automated, random access chemiluminescent enzyme immunoassay system. GOR antibody, which is often detected in the serum of patients infected withHepatitis C virus (HCV), is closely associated with HCV infection. This new assay provides detection of GOR antibody in 45 min, about half the time of existing EIA methods. The standard curve is 0.1-300 GOR unit/ml (1/10th-300 times cut-off value), giving a detection range about 30 times greater than that of existing assays. This greater detection","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1994-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735230","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1994-12-31DOI: 10.14921/JSCC1971B.23.4_323
G. Meng, F. Mashige, K. Maruyama, M. Nakano, A. Ohkubo
{"title":"Urinary Sulfated Bile Acids in Alcoholics","authors":"G. Meng, F. Mashige, K. Maruyama, M. Nakano, A. Ohkubo","doi":"10.14921/JSCC1971B.23.4_323","DOIUrl":"https://doi.org/10.14921/JSCC1971B.23.4_323","url":null,"abstract":"","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1994-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1994-12-31DOI: 10.14921/JSCC1971B.23.4_286
K. Takeuchi, Y. Matsuda, K. Miyazaki, R. Ishii, T. Hashimoto, S. Akihama
{"title":"Separation of Arginine Amidases Released from the Isolated Rabbit Aorta","authors":"K. Takeuchi, Y. Matsuda, K. Miyazaki, R. Ishii, T. Hashimoto, S. Akihama","doi":"10.14921/JSCC1971B.23.4_286","DOIUrl":"https://doi.org/10.14921/JSCC1971B.23.4_286","url":null,"abstract":"","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1994-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735184","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1994-12-31DOI: 10.14921/JSCC1971B.23.4_292
Kojiro Matsumoto, K. Negishi, M. Ishibashi, T. Ohtake, H. Yuki
{"title":"Antibody-Lectin Sandwich Enzyme Immunoassay for Determination of Altered Asparagine-Linked Sugar Chains in Serum Transferrin of Patients with Hepatoma","authors":"Kojiro Matsumoto, K. Negishi, M. Ishibashi, T. Ohtake, H. Yuki","doi":"10.14921/JSCC1971B.23.4_292","DOIUrl":"https://doi.org/10.14921/JSCC1971B.23.4_292","url":null,"abstract":"","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1994-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735219","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1994-09-30DOI: 10.14921/JSCC1971B.23.3_195
M. Kinoshita, T. Seno, Sadahito Shin, T. Aono
Polymorphisms of the genes for enzymes participating in the metabolism of several carcinogens have been identified. These polymorphisms are associated with varieties in the enzymatic activity or substrate specificity, and thus additive or multiplicative risks for development of various human cancers. In this study, we compared the genotype frequencies of four enzymes (CYP1A1, CYP2D6, N-acetyltransferase and glutathione S-transferase) from cervical cancer patients and healthy control individuals, to estimate the importance of polymorphisms in human papillomavirus infection and development of cervical cancer. The frequency of the Slow acetylator N-acetyltransferase genotype differed significantly between cervical cancer patients and healthy controls (P < 0.05, x2 = 4.24). No significant difference was found between these two groups in the frequency of any of the other genotypes studied. These findings suggest that the arylamine compounds metabolized by N-acetylation play an important role in human cervical carcinogenesis.
{"title":"Polymorphic Genotypes of Enzymes Involved in Carcinogen Metabolism as Risk Factors for the Development of Human Cervical Cancer","authors":"M. Kinoshita, T. Seno, Sadahito Shin, T. Aono","doi":"10.14921/JSCC1971B.23.3_195","DOIUrl":"https://doi.org/10.14921/JSCC1971B.23.3_195","url":null,"abstract":"Polymorphisms of the genes for enzymes participating in the metabolism of several carcinogens have been identified. These polymorphisms are associated with varieties in the enzymatic activity or substrate specificity, and thus additive or multiplicative risks for development of various human cancers. In this study, we compared the genotype frequencies of four enzymes (CYP1A1, CYP2D6, N-acetyltransferase and glutathione S-transferase) from cervical cancer patients and healthy control individuals, to estimate the importance of polymorphisms in human papillomavirus infection and development of cervical cancer. The frequency of the Slow acetylator N-acetyltransferase genotype differed significantly between cervical cancer patients and healthy controls (P < 0.05, x2 = 4.24). No significant difference was found between these two groups in the frequency of any of the other genotypes studied. These findings suggest that the arylamine compounds metabolized by N-acetylation play an important role in human cervical carcinogenesis.","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1994-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735173","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1994-06-30DOI: 10.14921/JSCC1971B.23.2_178
K. Seya, N. Ohkohchi, S. Mori
An improved colorimetric method for the determination of phosphatidylcholine hydroperoxide is described. Phosphatidylcholine hydroperoxide was allowed to react with potassium iodide in the presence of acetylchloride at room temperature, and the liberated iodine was measured colorimetrically at 550 nm after the addition of starch in 10% aqueous acetic acid. A linear response was observed between 5 and 40 nmol.
{"title":"An Improved Method for Determination of Phosphatidylcholine Hydroperoxide","authors":"K. Seya, N. Ohkohchi, S. Mori","doi":"10.14921/JSCC1971B.23.2_178","DOIUrl":"https://doi.org/10.14921/JSCC1971B.23.2_178","url":null,"abstract":"An improved colorimetric method for the determination of phosphatidylcholine hydroperoxide is described. Phosphatidylcholine hydroperoxide was allowed to react with potassium iodide in the presence of acetylchloride at room temperature, and the liberated iodine was measured colorimetrically at 550 nm after the addition of starch in 10% aqueous acetic acid. A linear response was observed between 5 and 40 nmol.","PeriodicalId":39360,"journal":{"name":"Japanese Journal of Clinical Chemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1994-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"66735162","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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