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Biomedical subjects

M Aoyama

Publications and source records attributed to M Aoyama.

At least 145 records · Page 8Linked to original sources
PubMed1982

[Chemotherapy of hepatocellular carcinoma--with special reference to one-shot intra-arterial infusion of a high dose of adriamycin].

Twenty-two cases of non-operable hepatocellular carcinoma (HCC) were treated with three types of chemotherapy mainly with Adriamycin (ADM). In the group (A), one shot intraarterial infusion of 100 mg ADM into the hepatic artery (9 cases), group (B), one shot intraarterial infusion of 30 mg ADM (3 cases), and group (C), 20-60 mg of systemic administration of ADM (10 cases) were examined. The therapeutic effects and side effects were studied comparatively among these three groups. In terms of tumor regression, RR was 4 cases (44.4%), and MR was 4 (44.4%) in group (A), and PR was 1 (10%) in group (C). The average survival time was 8.3 months (5 cases are still alive) in group (A), 5.7 months in group (B), and 4.2 months in group (C), respectively As side effects, alopecia was found 100% in (A), 33% in (B); leukocytopenia was found 100% in (A), 33% in (B); but no serious complication due to leukocytopenia was observed in any of them. One shot of 100 mg of ADM intraarterial infusion therapy seemed to be superior in therapeutic effects against HCC over other therapies.

Aged↗
PubMed1977

Amino acids and derivatives of thiazole-4-carboxylic acid as constituents of thiopeptin B.

L-Alanine, L-threonine, L-valine, D-cystine and three derivatives of thiazole-4-carboxylic acid (thiostreptin, 1-aminomethylthiazole-4-carboxylic acid and thiostreptoic acid) were isolated from the acid-hydrolysate of thiopeptin B. In addition, the presence of dehydrobutyrine and dehydroalanine residues in the antibiotic was determined. Other components remain unidentified.

Amino Acids↗
PubMed1975

Studies on trypsin inhibitor in barley. I. Purification and some properties.

To clarify the properties and functions of a trypsin inhibitor from Japanese barley in comparison with the inhibitor from Pirkka barley, an inhibitor was isolated from the barley Hordeum distichum L var. emend Lamark by extraction with 1% NaCl, ammonium sulfate fractionation and repeated chromatography on DEAE-cellulose and CM-cellulose. The final purified preparation of the inhibitor was found to be homogeneous by both chromatographic and electrophoretic analysis. The inhibitor was thermostable and was stable over the broad pH range from 2 to 11. No inhibition was observed by heavy metal ions and many reagents at 10(-2) M, except that p-chloromercuribenzoate caused a 69% loss of activity. The inhibitor was subjected to isoelectric focusing at pH 7.51 and its molecular weight was calculated to be 14,200+/-900 by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The apparent dissociation constant for the complex between the inhibitor and trypsin[EC 3.4.21.4] was 1.64 X 10(-7)M with casein as a substrate. One microgram of purified inhibitor inhibited 1.5 mug of pure trypsin in the hydrolysis of alpha-N-benzoyl-DL-arginine-p-nitroanilide. By chemical modification of arginyl residues in the inhibitor with 1,2-cyclohexanedione, the inhibitor was shown to be an arginine inhibitor. The inhibitor contained relatively many basic amino acids and few half cystines as compared with Pirkka barley trypsin inhibitor.

Amino Acids↗