著者
宮地 隆興 大庭 雄三
出版者
Japanese Electrophoresis Society
雑誌
生物物理化学 (ISSN:00319082)
巻号頁・発行日
vol.23, no.2, pp.175-178, 1979-09-25 (Released:2009-03-31)
参考文献数
15
著者
井上 勤 浅賀 宏昭 田村 真弓
出版者
Japanese Electrophoresis Society
雑誌
生物物理化学 (ISSN:00319082)
巻号頁・発行日
vol.30, no.3, pp.229-238, 1986-05-31 (Released:2009-03-31)
参考文献数
19
被引用文献数
1 1
著者
高月 清
出版者
日本電気泳動学会
雑誌
生物物理化学
巻号頁・発行日
vol.42, no.2, pp.73-77, 1998

DNAからRNAへの読み取りとは逆方向の転写を行う酵素, すなわち逆転写酵素をもつウイルスを総称してレトロウイルスという. ヒトの疾患の病因ウイルスとしてはHTLV-1とHIVがある. それぞれ成人T細胞白血病 (ATL) とエイズの病原体である. ATLは日本で発見記載された疾患であり, 九州, 沖縄などに多い. エイズは1980年代に全世界に拡がり人類の脅威として恐れられている. この2つの疾患について疫学, 病像, 診断, 検査, 予防と治療を解説した. 現代の医学ではまだ解決しないが, 研究の進歩により曙光のみえてきた部分もある.
著者
縄田 修吾 加藤 紘 中村 和行
出版者
Japanese Electrophoresis Society
雑誌
生物物理化学 (ISSN:00319082)
巻号頁・発行日
vol.42, no.4, pp.257-263, 1998-12-15 (Released:2009-03-31)
参考文献数
10
被引用文献数
1

Recently, tumor markers, which have been developed for the diagnosis and evaluation for cancer, are regarded as new key tools to study the malignant behavior of cancer, and therefore, much attension has been focused on their biological functions. Squamous cell carcinoma (SCC) antigen is a tumor marker of SCC arising in various sites. We have investigated the biological function and heterogeneity of this tumor marker by electrophoretic methods. In this paper, we report that SCC antigen belongs to the inhibitory type of serine protease inhibitor family, indicating that SCC antigen may affect malignant behavior such as tumor invasion. We also describe the different pattern of SCC antigen by two-dimensional electrophoresis in normal and cancer tissues, and indicate that the heterogeneity of SCC antigen results mainly from the presence of two homologous genes, SCCA 1 and SCCA 2 gene.

1 0 0 0 OA 学問の喜び

著者
廣中 平祐
出版者
日本電気泳動学会
雑誌
生物物理化学 (ISSN:00319082)
巻号頁・発行日
vol.44, no.2, pp.53-57, 2000-06-15 (Released:2009-03-31)
著者
山田 尚之 窪田 和幸 河上 麻美 中山 聡 鈴木 榮一郎
出版者
日本電気泳動学会
雑誌
生物物理化学 (ISSN:00319082)
巻号頁・発行日
vol.52, no.2, pp.25-30, 2008 (Released:2009-12-04)
参考文献数
20

Genomics and proteomics have been useful in many different areas of medicine and health science as an aid to discover new biomarker for disease diagnosis or staging and as a tool to predict or monitor treatment response or toxicity. Human serum albumin (HSA) exists in both reduced and oxidized forms, and the percentage of oxidized albumin increases in several diseases. However, little is known regarding the pathological and physiological significance of oxidation due to poor characterization of the precise structural and functional properties of oxidized HSA. Here, we characterize both the structural and functional differences between reduced and oxidized HSA. Using LC-ESI TOF MS and FT MS analysis, we determined that the major structural change in oxidized HSA in healthy human plasma is a disulfide-bonded cysteine at the thiol of Cys34 of reduced HSA. Based on this structural information, we prepared standard samples of purified HSA, e.g. non-oxidized (intact purified HSA which mainly exists in reduced form), mildly oxidized and highly oxidized HSA. Using these standards, we demonstrated several differences in functional properties of HSA including protease susceptibility, ligand-binding affinity and antioxidant activity. From these observations, we conclude that an increased level of oxidized HSA may impair HSA function in a number of pathological conditions. In addition, we determined blood and plasma sampling conditions for the accurate measurement of the oxidized albumin ratio in plasma by using EST-TOF MS screening.