DSpace コレクション: 1989-041989-04http://hdl.handle.net/10564/22622024-03-28T18:12:37Z2024-03-28T18:12:37Z2種の異種抗体を用いたELISAによるα₂-アンチプラスミン抗原量の測定松岡, 宏明橋本, 憲治金廣, 照美福井, 弘高瀬, 俊夫杉本, 充彦三上, 貞昭http://hdl.handle.net/10564/22922017-05-29T06:08:56Z1989-04-29T15:00:00Zタイトル: 2種の異種抗体を用いたELISAによるα₂-アンチプラスミン抗原量の測定
著者: 松岡, 宏明; 橋本, 憲治; 金廣, 照美; 福井, 弘; 高瀬, 俊夫; 杉本, 充彦; 三上, 貞昭
抄録: A new solid enzyme-linked immunosorbent assay (ELISA) for human α₂-antiplasmin (α₂-AP) antigen was developed using two kinds of anti-human α₂-AP antiserum. The procedure of α₂-AP antigen assay is as follows : Step 1 ; a microtiter plate is coated with an anti-human α₂-AP guineapig antiserum for 24 hrs at 4℃. Step 2 ; serially diluted plasma is added to the plate and incubated for 24 hrs at 4℃. Step 3 ; after washing with a phosphate buffered saline, an anti-human α₂-AP rabbit antiserum is added to the plate and incubated for 3 hrs at 37℃. Then, a peroxidase conjugated anti-rabbit IgG goat antiserum is added and incubated for 1 hr at 37℃. After the 3rd step, the microtiter plate is washed extensively. Finally, the α₂-AP antigen is determined by ELISA method using o-phenylendiamin as the substrate. The lower limit of α₂-AP antigen in this assay was 0.1 U/dl. In 25 healthy adult males and 25 adult females, the mean values of α₂-AP were 96.8±12.2 U/dl and 95.2±10.7 U/dl, respectively. A good correlation was found between the α₂-AP level determined by this ELISA method and by Laurell's method. There was also a good correlation between α₂-AP activity by an amidolytic method and antigen level by the ELISA.1989-04-29T15:00:00Z新生児期のα₂-アンチプラスミンの動態 : 成熟児・未熟児の新生児期におけるα₂-アンチプラスミンの推移松岡, 宏明http://hdl.handle.net/10564/22852017-05-29T06:09:30Z1989-04-29T15:00:00Zタイトル: 新生児期のα₂-アンチプラスミンの動態 : 成熟児・未熟児の新生児期におけるα₂-アンチプラスミンの推移
著者: 松岡, 宏明
抄録: Levels of α₂-antiplasmin activity (α₂-AP : C) and antigen (α₂-AP : Ag) were measured in 50 normal full-term and 21 premature newborn infants during the first month of life. In full-term infants, the α₂-AP : Ag levels were assayed by electro immuno assay (EIA) and enzyme-linked immunosorbent assay (ELISA). The mean values of α₂-AP : C, α₂-AP : Ag-EIA and α₂-AP : Ag-ELISA were lowest on the first day of life, i. e., 59.5±8.8 u/dl, 61.3±7.1 u/dl and 60.8±9.2 u/dl respectively. The values gradually increased during the first month, reaching 96.2±8.3 u/dl, 99.2±7.1 u/dl and 97.7±8.0 u/dl respectively. Premature infants were divided into three groups based on their birth weight : Group A of 2001-2500 g ; Group B of 1501-2000 g ; Group C of below 1500 g. In Group A, the mean values of α₂-AP : C and α₂-AP : Ag on the first day of life were 59.0±10.0 u/dl and 60.2±9.1 u/dl. The values gradually increased during the first month, reaching 90.6±9.2 u/dl, 91.0±13.8 u/dl respectively. These levels were almost the same as those of full term infants. In Group B, the mean values on the first day of life were 57.2±11.8 u/dl and 56.8 u/dl respectively. These levels moderately increased during the first month, showing 77.8±9.8 u/dl, 75.8±6.8 u/dl. These levels were lower than those of Group A. In Group C, these levels on the first day of life were 56.1±9.3 u/dl and 55.8±7.4 u/dl. These levels slightly increased during the first month, showing 65.5±13.7 u/dl, 66.6±12.8 u/dl respectively. These levels were apparently lower than those of Group A and B. There was no significant difference in α₂-AP : C and α₂-AP : Ag in their samples.1989-04-29T15:00:00Zコラーゲン様補体成分C1qの構造と機能に関する研究 : ウシおよびヒトC1qの比較研究佐々木, 隆子http://hdl.handle.net/10564/22842017-08-10T02:48:21Z1989-04-29T15:00:00Zタイトル: コラーゲン様補体成分C1qの構造と機能に関する研究 : ウシおよびヒトC1qの比較研究
著者: 佐々木, 隆子
抄録: In order to find a clue to the molecular evolution mechanism of collagen-like molecules, comparative studies on the function and the structure of human and bovine C1q, a collagen-like complement component, were carried out. The hemolytic activity of bovine C1q was conspicuously higher than that of human C1q. On the other hand, the ability of bovine C1q to bind to Fc of immune complexes was a little lower than that of human C1q. However, these activities were interchangeable between them.
Both the N-terminal collagen-like (CLF) and the C-terminal globular fragments (GF) of these C1q were highly purified by enzymic digestion followed by gel filtration, and their physicochemical and antigenic characterization was performed. Polyacrylamide gel electrophoresis (PAGE) analyses have shown that not only whole molecules of both C1q but also CLFs and GFs seem to be composed of essentially the same peptide structures. Some similarities between amino acid compositions of both CLFs and great similarities between those of both GFs were found. Moreover, great similarities of amino acid compositions were found among three non-covalently linked chains of each GF as well as between the corresponding chains of both GFs. Immunodiffusion analyses and radioimmune inhibition tests have shown that the definitive antigenic cross-reactivity is present between these two C1q molecules, and that the regions participating in interspecies cross-reactions are located in both CLF and GF of C1q. These results suggest that both CLF and GF on the C1q molecule remained highly conserved in their evolution, and that the hemolytic activity and the Fc-binding ability
evolved independently to some extent. The possible relation of the C1q evolution to that of collagen molecules has been also discussed.1989-04-29T15:00:00Z加熱第Ⅷ因子濃縮製剤,Haemate Pの止血管理下に抜歯を行ったType ⅡB von Willebrand病の1例田中, 一郎新家, 興宮田, 茂樹西尾, 健治吉岡, 章福井, 弘藤村, 吉博山本, 成美杉村, 正仁http://hdl.handle.net/10564/22832017-06-11T23:20:26Z1989-04-29T15:00:00Zタイトル: 加熱第Ⅷ因子濃縮製剤,Haemate Pの止血管理下に抜歯を行ったType ⅡB von Willebrand病の1例
著者: 田中, 一郎; 新家, 興; 宮田, 茂樹; 西尾, 健治; 吉岡, 章; 福井, 弘; 藤村, 吉博; 山本, 成美; 杉村, 正仁
抄録: A dental surgery case is described of a 12-year-old boy with type ⅡB von Willebrand's disease (vWD), suffering from toothache caused by follicular cyst with infection in the mandible. Prior to the surgery, a hemostatic effect of Haemate P was studied. After the infusion of Haemate P (84 U/kg body weight of ristocetin cofactor (Rcof.) ; 28 U/kg of factor Ⅷ activity (F. Ⅷ : C)), F. Ⅷ : C levels rose from 0.6 U/ml to 1.64 U/ml at 1 hour, 1.08 U/ml at 24 hours and 0.9 U/ml at 48 hours, respectively. The levels of Rcof. inreased from 0.24 U/ml to 2.75 U/ml at half an hour after the infusion and then gradually decreased to 0.44 U/ml at 48 hours. The levels of botrocetin cofactor (Bcof.) increased from 0.4 U/ml to 2.6 U/ml at half an hour after the infusion and then gradually decreased to the preinfusion level at 48 hours. Before the infusion, the large multimers were absent in the plasma, whereas all multimers were present in the platelets. After the infusion, the large multimers in the plasma appeared for several hours and gradually disappeared at 48 hours. Surgical procedures - an extirpation of the cyst in the mandibular bone and the extractions of 3 deciduous teeth (both sides of the second mandibular lower deciduous molars and the right upper second deciduous molar) and 1 supernumerary tooth in the maxilla ― were
performed after the infusion of Haemate P (56 U/kg body weight of Rcof. ; 18 U/kg body weight of F. Ⅷ : C). Further infusions of Haemate P were given every 12 hours for 2 days and every 24 hours for the following 3 days. After each infusion of Haemate P, there was 2-3 fold increase of 3 activities of F. Ⅷ/vWF. During the course of Haemate P infusions, there was no significant side effect.1989-04-29T15:00:00Z