順天堂医学
Online ISSN : 2188-2134
Print ISSN : 0022-6769
ISSN-L : 0022-6769
18 巻, 1 号
選択された号の論文の16件中1~16を表示しています
目次
特集:悪性腫瘍と外科(第178回学術集会)
原著
  • 八田 賢明
    1972 年 18 巻 1 号 p. 97-99
    発行日: 1972年
    公開日: 2014/11/22
    ジャーナル フリー
    The incidence of calcification in uterine myomata is 1-3%. Most of these patients do not manifest clinical symptoms and on many occasions are only discovered as incidental findings at the time of X-ray examination, operation and autopsy. With X-ray evalution and internal, examination the author recently made a diagnosis of calcification of a uterine myoma in a patient complaining of hypogastric pain which was confirmed at operation and has reported the case.
  • P22 Phage coat proteinの3分画の免疫活性 (その2)
    堀越 美智子, 上条 清明
    1972 年 18 巻 1 号 p. 100-105
    発行日: 1972年
    公開日: 2014/11/22
    ジャーナル フリー
    Rabbits were immunized with F1, F2, and F3, respectively and the precipitin titers and K-values were tested with reference to the protein amounts used. Results obtained were summarized as follows : 1) The lethal effect was seen in P22 protein, F1 and F2, i.e., rabbits died with subcutaneous injection of 0.09-1.8mg of them. On the other hand, the necessary doses of the protein preparations to obtain sufficient titers of antibodies ranged from 0.8mg to 2.0mg. The preparations were injected subcutaneously in 4-5 times and dosis per injection was 0.3mg or 0.4mg. With these doses, some of the animals died after 1 or 2 injections. 2) Among the three fractions, only F3 was the fraction markedly relating to the production of the neutralizing antibody. 3) Precipitin was produced equally in animals injected with any of the three fractions, but with the equal amount of antigen, it was most marked with F1 and was followed by F2 and F3. 4) The neutralizing antibody was produced, also, with F2, but the titer was low and disappeared in a short period of time.
  • P22 phage coat protein 3 分画の分子構造 (その1)
    堀越 美智子, 上条 清明
    1972 年 18 巻 1 号 p. 106-111
    発行日: 1972年
    公開日: 2014/11/22
    ジャーナル フリー
    Amino acid analysis, N-terminal determination, reductive cleavage of the S-S bond with mercaptoethanol and the estimation of the molecular weight were carried out with the 3 fractions of P22 phage coat protein. Results obtained were summarized as follows : 1) It was suggested that F1, F2 and F3 differed even in their primary molecular structure. 2) The molecular weight of F1, F2 and F3 were 125,000, 39,000 and 32,000, respectively, so far estimated by the method of Shapiro et al. 3) From the amino acid molar ratio, the molecular weights were caculated as 122,000. for F1 and 25,650 for F3. 4) N-terminal amino acid was valine samely in F1, F2 and F3, irrespective of their difference in immunresponse and presumed molecular structure. 5) After cleavage of the S-S bond by treatment with mercaptoethanol, F1 showed almost same migration as the original F1 molecule, whereas F2 and F3 showed slower migration than originals. This facts show the difference in secondary or tertiary molecular configuration of the three fractions, especially with refference to the intermolecular S-S bonds.
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