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Biomedical subjects

T Sugimura

Publications and source records attributed to T Sugimura.

At least 955 records · Page 53Linked to original sources
PubMed1976

Beta-glucuronidase isozyme patterns of experimental hepatomas of rats.

Beta-Glucuronidase isozymes in rat tissues were separated by electrophoresis on cellulose acetate membranes. Using this method, beta-glucuronidase isozyme patterns were studied in normal rat liver and experimental hepatomas with different growth rates. Changes of isozyme patterns during postnatal development were also studied in rat liver. Normal rat liver contained six types of beta-glucuronidase, numbered I to VI in order to decreasing mobility to the cathode. Type II beta-glucuronidase stained most intensely and was detected in all the cells examined. The isozyme patterns of Morris hepatomas, which are slowly growing and not highly deviated, resembled that of normal rat liver but lacked definite Type III beta-glucuronidase. Yoshida ascites hepatomas, which are rapidly growing and highly deviated, contained only Type II, but some had Types II, V, and VI beta-glucuronidase. Embryonal liver just before birth contained only Type II, but with increase in activity during development after birth, minor bands of Type I and Types III to VI beta-glucuronidase appeared successively to complete the adult pattern.

Animals↗
PubMed1976

Typing foot-and-mouth disease virus by fluorescent antibody technique.

Typing of foot-and-mouth disease (FMD) virus was performed by the direct fluorescent antibody (FA) technique. Type-specific FA was prepared from the following two sorts of procedures: (1) FA against live virus (FA-live) was prepared from hyperimmune serum taken from guinea pigs having received live FMD virus. Then it was adsorbed with concentrated heterotype antigen. (2) FA against inactivated virus (FA-Inact) was prepared from antiserum taken from guinea pigs immunized with purified FMD virus inactivated with acetylethyleneimine. Seventeen strains of FMD virus (seven strains of type A, seven strains of type O, and three strains of thpe C) were used. Type-specific FMD virus antigen was detected distinctly from the monolayer of BHK cells infected with each type of virus and fixed in acetone, in spite of negative results obtained from the cells fixed in methyl alcohol. All the 17 strains were typed successfully by the implementation of these two FA methods.

Aphthovirus↗
PubMed1976

[Experimental gastric cancer (author's transl)].

Methods have been established to produce gastric cancer in rats and dogs by administration of N-methyl-N'-nitro-N-nitrosoguanidine or of the ethyl derivate. The agent is administered in drinking water or by a pellet diet soaked in the carcinogen. Histologically well differentiated and poorly differentiated types of adenocarcinoma and signet-ring cell tumors are induced in several months with greath reliability. Metastases were observed in both rats and dogs with gastric carcinoma. The carcinogenic effect could be enhanced by surface active agents, sodium chloride, iodoacetamide, insertion of plastic beads into the stomach and gastroenteroanastomosis. Follow-up studies by radiologic, endoscopic and bioptic examinations are possible in the dog. There are similarities in these experimental tumors to those in man and thus they provide means for the investigation of histogenesis, prevention, and chemotherapy of gastric cancer. An adenocarcinoma of the glandular stomach of a Wistar rat was successively transplanted to new born rats of the same strain.

Adenocarcinoma↗
PubMed1975

Comparative studies on electrophoretic mobility and immunogenicity of pancreatic and parotid amylases of rat.

1. The alpha-amylases (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) of rat serum, urine, pancreas, parotid gland and liver were separated by electrophoresis on a cellulose acetate membrane. They were found to be of three different types: a parotid gland type, a pancreatic type and a liver type. Rat serum and urine contained parotid type amylase only. 2. Antisera were prepared in rabbits against purified rat pancreatic amylase and parotid amylase. In addition to strong reactions between pancreatic amylase and its antiserum and between parotid amylase and its antiserum, a weak cross-reaction was observed between parotid amylase and anti-pancreatic amylaseserum. Anti-parotid-amylase serum gave an immunoprecipitation line with rat serum and urine, but anti-pancreatic-amylase serum did not, indicating that the amylases in serum and urine originate from parotid amylase.

Amylases↗
PubMed1975

Electrophoretic and immunological properties of liver alpha-amylase of well-fed and fasted rats.

1. Alpha-Amylase (1,4-alpha-D-glucan glucanohydrolase, EC 3.2.1.1) in the liver of well-fed rats showed a characteristic electrophoretic mobility between those of pancreatic and parotid amylases. Amylase in the liver of fasted rats showed an electrophoretic mobility identical to that of parotid amylase. When fasted rats were re-fed on a standard diet for two days the electrophoretic mobility of their liver amylase returned to that of the liver amylase of well-fed rats. 2. When purified rat pancreatic and parotid amylases were mixed with a final concentration of 4% glycogen solution, their electrophoretic mobilities both became similar to that of liver amylase of well-fed rats. The electrophoretic mobility of glycogen corresponded to that of liver amylase of well-fed rats. Since liver amylase of fasted rats has the same mobility as parotid amylase and serum contains only parotid-type amylase, these findings suggest that liver amylase of well-fed rats may be a complex of serum amylase and glycogen. 3. The antigenicities of the liver amylases of well-fed and fasted rats were the same as that of purified parotid amylase, but different from that of purified pancreatic amylase. Amylase in serum and urine, which had the same electrophoretic mobility as parotid amylase, had the same antigenicity as purified parotid amylase and the liver amylases of well-fed and fasted rats.

Amylases↗
PubMed1975

Purification and properties of alpha,alpha-trehalase from the mucosa of rat small intestine.

ALPHA,ALPHA-Trehalase (EC 3.2.1.28, alpha,alpha-trehalose glucohydrolase) was solubilized from the microvillous membrane of the intestinal mucosa of rats with Triton X-100 and butanol. It was purified 6350-fold by gel filtration on Sephadex G-150 and chromatography on DE-52 and hydroxyapatite. The purified enzyme, with a specific activity of about 127 units per mg of protein, showed almost a single band of protein and activity on polyacrylamide gel electrophoresis. Its molecular weight was estimated to be 96 000 on Sephadex G-150 and 90 000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Its pH optimum was 5.5-5.7 and its Km value for trehalose was 5.4 mM. Its activity was inhibited 30 and 100% by 1 mM p-chloromercuribenzoate and 0.1 mM HgCl2, respectively and 30% by 1 mM MgCl2. Moreover, its activity was inhibited completely by 10 mM tris(hydroxymethyl)aminomethane and about 60% by 10 mM sucrose and cellobiose. The enzyme showed a high specificity for trehalose.

Animals↗
PubMed1975

Separation of human alpha-amylase isozymes by electro-focusing and their immunological properties.

Human alpha-amylase (alpha-1,4-glucan-4-glucanohydrolase, EC 3.2.1.1) was separated by electrofocusing. The amylases in serum and urine were seperated into two major isozymes with isoelectric points of pH 6.4-6.5 and pH 6.9-7.0, respectively, and one minor isozyme with an isoelectric point of pH 5.9. The amylases in saliva were separated into one major isozyme with an isoelectric point of pH 6.5 and two minor isozymes with isoelectric points of pH 6.0 and 6.9. The amylases in pancreatic juice gave one major peak at pH 7.0 and two minor peaks at pH 6.0 and pH 6.5. Repeated electrofocusing of each isozyme have only a single peak with a constant isoelectric point. The antigenicites of these three isozymes were also investigated using antisera to rat pancreatic and parotid amylases.

Amylases↗
PubMed1975

Correlation between the carcinogenicities of nitrofuran derivatives and their destructive actions on sebaceous glands of mouse skin.

The effects of six nitrofuran derivatives (including a formerly used food preservative) on mouse skin sebaceous glands were investigated. A close correlation was found between the carcinogenicities and destructive activities of nitrofuran derivatives on the sebaceous glands. 5-Nitro-2-furaldehyde semicarbazone and 4-methyl-1-[(5-nitrofurfurylidene)amino]-2-imidazolidinone, which are carcinogenic, caused marked destruction of the glands at a dose of 1-5 mg/mouse. 2-(5-Nitro-2-furfurylidene)-aminoethanol almost completely destroyed the glands at a dose of 5 mg/mouse; its carcinogenicity has not yet been investigated. 1-[(5-Nitrofurfurylidene)amino]-carcinogenic, did not affect the glands, even at a dose of 5 mg/mouse. 2-(2-Furyl)-3-(5-nitro-2-furyl)acrylamide, which is a potent mutagen but not carcinogenic, had no effect on the glands at a dose of 5 mg/mouse. Under similar conditions, the potent carcinogen 7,12-dimethylbenz(alpha)athracene almost completely destroyed the sebaceous glands at a dose of 0.05 mg/mouse, but dimethyl sulfoxide (used as solvent for the test compounds) had no effect.

Animals↗