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Featured researches published by Daiichi Kakimoto.


Microbiology and Immunology | 1985

Potentiality of Artificial Sea Water Salts for the Production of Carrageenase by a Marine Cytophaga sp.

Golam Sarwar; Hiroshi Oda; Taizo Sakata; Daiichi Kakimoto

Production of an extracellular enzyme complex (carrageenase) was studied by examining cell‐free fluids from cultures of a marine Cytophaga, 1k‐C783, growing on different media.


Nippon Suisan Gakkaishi | 1979

Studies on the flagellation of marine Vibrio, B-1 strain isolated from kinko bay.

Kunihiko Nakamura; Daiichi Kakimoto; James R. Swafford; Roy M. Johnson

A bacterial strain B-1 isolated from the seashore was identified as V. alginolyticus. This strain, marine halophilic bacterium, was examined by means of electron microscopy, to observe the fine structure and the flagella. The bacterium had a single polar flagellum when grown in a liquid medium and had peritrichous flagella when grown on a solid medium. In liquid medium, several bleb-like tubular structures originating from the cell wall were often observed. These seem to be immature and intermediate forms of flagella. The flagella number and the body length of the strain increase with incubation time on agar plates.


Nippon Suisan Gakkaishi | 1977

Studies on malate dehydrogenases of marine bacteria. I. Comparison between marine and terrestrial species.

Michiko Inai; Taizo Sakata; Daiichi Kakimoto

The activities of various malate dehydrogenases (MDH and malic enzymes) were studied by comparing marine Pseudomonads and Vibrios with their terrestrial counterparts and with fish intestinal isolates. In addition, the relationship between the enzyme activity produced under cultivation and the NaCl concentration in the culture medium was studied. The medium used was ZoBell 2216E, the NaCl varying in concentration from 0.5 to 7%. The results showed that the activities of both MDH and malic enzymes varied in accordance with genera and with habitat, while NaCl exerted little effect in any of the strains.


Nippon Suisan Gakkaishi | 1974

Studies on the electrophorsis of marine bacterial enzymes - II esterase, malate dehydrogenase, and Lactate dehydrogenase.

Michiko Inai; Taizo Sakata; Daiichi Kakimoto

Electrophoretic zymograms of the three enzymes, esterase, malate dehydrogenase (MDH), and lactate dehydrogenase (LDH) were determined for 11 strains of marine isolates. For comparison, some terrestrial bacteria of the same or similar genera were also analyzed. The results obtained indicated that there were zymographic differences between the various genera, irrespective of the enzymes concerned. Clear differences in both esterase and MDH isozyme-zymograms were noticed between the marine and terrestrial specimens of Pseudomonas.


Nippon Suisan Gakkaishi | 1960

STUDIES ON THE UNKNOWN FACTOR IN THE PYLORIC COECA OF SKIPJACK-III

Daiichi Kakimoto

1. At variance with the known CF which readily loses the power of promoting the growth of Leuconostoc citrovorum after being kept at a pH lower than 2.0, the unknown factor is not damaged of its activity toward this microorganismus even when exposed to any pH in the range from 1.0 to 14 (Table 1). 2. The unknown factor is comparatively unstable to a strong acid. It loses said promotive power to some extent when boiled in 5% H2SO4 and is completely invalidated by heating with 25% H2SO4 (Fig. 2 and 4). On the other hand, the unknown factor remains comparatively stable against a strong alkali. Its characteristics toward Leuc. citrovorum are not damaged even when kept in contact with 10% KOH (see Fig. 3). In this connection, the response of Leuc. citrovorum to the unknown factor appeared to be more or less strongly suppressed in the presence of salt inevitably ensuing from the neutralization of the agent employed in acidification or alkalization. 3. The unknown factor can be selectively adsorbed on an ion-exchange resin, only when the resin is of strong acid form (see Table 2 and Fig. 5). It can also be desorbed from the exchanger by means of 0.5N NaOH. 4. The unknown factor itself could not be precipitated by the addition of any agent thus far tested. 5. A crude preparation of the unknown factor was positive to diazo reaction, Morlishs reaction and Folins reaction, but negative to ninhydrin reaction (Table 4).


Nippon Suisan Gakkaishi | 1956

Studies on the Utilization of Pyloric Coeca of Skipjack-II

Daiichi Kakimoto; Tetsuro Yoshimine

In the isolation of arginine from extractive matter of pyloric coeca, it is necessary to find means for elimination of agmatine. Basic nitrogen compounds containing arginine and agmatine were separated from other matters by the treatment with activated charcoal at pH 8.0 followed by the elution with HCl-acetone. After removed of acetone the residue was treated with picric acid, almost all the agmatine being precipitated. After filtyering off the agmatine picrate, arginine was precipitated as its flavianate, and finally purified as the hydrochloride. The yield of arginine thus obtained corresonded to 76% by the bioassay value.


Nippon Suisan Gakkaishi | 1952

A New Method for the Determination of Gelatin-I

Ken-ichi Kashiwada; Daiichi Kakimoto

普通の蛋白質が三塩化酷酸によつて洗澱し,ペプトン等の誘導蛋白質は中性醋酸鉛によつて沈澱するが,ゼラチンは此等の試薬によつて全く沈澱せずしてFOLIN-WU試薬によつて定量的に沈澱し,且つ此の試薬によつてアミノ酸,有機塩基,その他の低分子窒素化合物の沈澱しない性質を利用したゼラチンの一新定量法を考案した。本法は操作も簡易で長時聞を要せず,且つ従来の方法に比較し一層正確な値を与えることを知つた。 終りに本研究を行ろに当り分析の一部を実施された肥後一馬氏,西尾米子嬢に厚く感謝の意を表する。


Nippon Suisan Gakkaishi | 1980

Variations in the intestinal microflora of Tilapia reared in fresh and sea water.

Taizo Sakata; Jun Okabayashi; Daiichi Kakimoto


Journal of Applied Microbiology | 1994

Characterization of an antibiotic produced by Alteromonas luteoviolacea Gauthier 1982,85 isolated from Kinko Bay, Japan

Susan A. McCARTHY; Roy M. Johnson; Daiichi Kakimoto


Nippon Suisan Gakkaishi | 1980

Microflora in the gastrointestinal tracts of freshwater fish - I. Isolation and distribution of obligate anaerobic bacteria from the intestines of freshwater fish.

Taizo Sakata; Haruo Sugita; Tomotari Mitsuoka; Daiichi Kakimoto; Hajime Kadota

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Roy M. Johnson

Arizona State University

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