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Biomedical subjects

J Shoji

Publications and source records attributed to J Shoji.

At least 73 records · Page 4Linked to original sources
PubMed1981

Structural studies on thiocillins I, II and III (studies on antibiotics from the genus Bacillus XXIX).

Thiocillins I, II and III were compared with micrococcin P1 by analysis of acid hydrolyzates of the native and the reduced antibiotics as well as by means of 1H and 13CNMR spectroscopies. As a result of these studies, the differences of these antibiotics were clarified in their structural units, and the structures of thiocillins I, II and III were assigned on the basis of the proposed structure of micrococcin P1.

Anti-Bacterial Agents↗
PubMed1981

Isolation of N-(2,6-diamino-6-hydroxymethylpimelyl)-L-alanine from Micromonospora chalcea.

A novel dipeptide, N-(2,6-diamino-6-hydroxymethylpimelyl)-L-alanine, was isolated from the culture broth of a microorganism identified as Micromonospora chalcea. The dipeptide exhibits antimicrobial activity against Escherichia coli on a synthetic medium, and the activity is synergistically enhanced by several cell wall synthesis-inhibitors.

Amino Acids, Diamino↗
PubMed1980

Isolation of octapeptin D (studies on antibiotics from the genus Bacillus. XXVII).

A new peptide antibiotic complex, named octapeptin D, was isolated from culture broth of a microorganism belonging to the genus Bacillus. The trihydrochloride of the antibiotic was obtained as a colorless powder, soluble in water and methanol. The empirical formula, C47H88N12O11.3HCl.H2O, was indicated by elemental analysis. Amino acid analysis on the acid hydrolyzate demonstrated the presence of 2,4-diaminobutyric acid (4 moles), serine (1 mole) and leucine (3 moles). Gas chromatographic analysis with the methylated product of the ethereal extract of the acid hydrolyzate revealed the presence of beta-hydroxy isodecanoic acid, beta-hydroxy decanoic acid, beta-hydroxy isoundecanoic acid and beta-hydroxyanteisoundecanoic acid. Octapeptin D is active against Gram-negative and Gram-positive bacteria in vitro and in vivo.

Animals↗
PubMed1979

The structures of tridecaptins B and C (studies on antibiotics from the genus Bacillus. XXV).

On examining the structures of the antibiotics tridecaptins B and C, the constituent amino acids were separated and their chiralities were determined. The constituent fatty acids were identified by gas chromatography and mass spectrometry. Cleavage with N-bromosuccinimide and sequential analysis by EDMAN degradation demonstrates the sequence of the C-terminal side of tridecaptins B and C. Deacylation with polymyxin acylase of tridecaptin B and successive EDMAN degradation revealed the sequence of the N-terminal side of tridecaptin B. Finally partial acid hydrolysis on tridecaptin C clarified the sequence of the N-terminal side of tridecaptin C.

Amino Acids↗
PubMed1979

Resolution of peptide antibiotics, cerexins and tridecaptins, by high performance liquid chromatography (studies on antibiotics from the genus Bacillus. XXVI).

By high performance liquid chromatography, cerexin B was separated into four components (B1, B2, B3 and B4), cerexin D into four components (D1, D2, D3 and D4), tridecaptin A into components (A alpha and A beta), tridecaptin B into four components (B alpha, B beta, B gamma and B delta) and tridecaptin C into three components (C alpha 1, C alpha 2 and C beta 1). All components were preparatively isolated, and their fatty acid and amino acid compositions determined for structural elucidation.

Amino Acid Sequence↗
PubMed1979

Enhancement and suppression in production of IgM-antibody in mice treated with purified saponins.

Effects of purified saponins on antibody production against SRBC antigen were investigated in adult mice by using the direct hemolytic plaque technique of Cunningham and Szenberg. Intravenous injection of ginsenoside-Rb1, -Rc, senegin-III, -IV or platycodin-D caused increase in antibody-producing cells. However, the same treatment with ophiopogonin-D, ginsenoside-Rd or glycoside-H2 suppressed antibody production. Immuno-suppression due to the latter three substances seemed not to be associated with cytocidal effect. Ophiopogonin-B and platycodin-C had no effects.

Animals↗
PubMed1978

The structure of tridecaptin A (studies on antibiotics from the genus Bacillus. XXIV).

On examining the structure of the antibiotic tridecaptin A, the constituent amino acids were determined to be: 2,4-diaminobutyric acid(2D, 1L), Ser(1D, 1L), Glu(1L), Gly(1), Ala(1L), Val(1D, 1L), aIle(1D), Phe(1L) and Trp(1D). The constituent fatty acid was identified as beta-hydroxy anteisononanoic acid by gas chromatography and mass spectrometry. Cleavage reaction with N-bromosuccinimide, sequential analysis by EDMAN degradation, partial acid hydrolysis and some additional evidences clarified the structure of tridecaptin A.

Amino Acid Sequence↗