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Biomedical subjects

J Shoji

Publications and source records attributed to J Shoji.

At least 109 records · Page 6Linked to original sources
PubMed1976

Isolation of a new antibiotic 333-25, related to antibiotic EM 49. (Studies on antibiotics from the genus Bacillus. XI).

A new antibiotic, 333-25, active against Gram-positive and Gram-negative bacteria, was isolated from the culture broth of Bacillus circulans 333-25. The antibiotic is a basic acylpeptide containing 2,4-diaminobutyric acid (5), leucine (2), phenylalanine (1) and a fatty acid. It is closely related to antibiotic EM 49, but can be differentiated by chromatographic behaviour.

Animals↗
PubMed1976

The constituent amino acids and fatty acid of antibiotic 333-25. (Studies on antibiotics from the genus Bacillus. XII.

Measurement of the optical rotational activities of the constituent amino acids of antibiotic 333-25 identified 2,4-diaminobutyric acid (D-form 1, L-form 4), L-leucine (2) and D-phenylalanine (1). The fatty acid constituent was determined to be beta-hydroxy anteisononanoic acid by gas chromatography, nuclear magnetic resonance and mass spectra. Differentiation from the structure of antibiotic EM 49 is discussed.

Amino Acids↗
PubMed1976

Isolation of a new peptide antibiotic complex, B-43 (studies on antibiotics from the genus Bacillus. XV).

A new peptide antibiotic complex B-43, active against Gram-positive and Gram-negative bacteria, was isolated from a strain of Bacillus circulans. This antibiotic contains aspartic acid, valine, isoleucine, leucine, phenylalanine and 2,4-diaminobutyric acid. It seems to be related to polypeptin and antibiotic complex 4205, but differs in that it contains aspartic acid residue.

Animals↗
PubMed1975

Isolation of galantins I and II, water-soluble basic peptides. Studies on antibiotics from the genus Bacillus. III.

Two water-soluble basic antibiotics named galantins I and II were isolated from a strain resembling Bacillus pulvifaciens. Both antibiotics are peptides containing glycine, alanine, ornithine, lysine and some unknown ninhydrin-positive components. An approximate empirical formula C50 plus and minus H98plus and minus 2O17N16 is indicated for galantin I. These are active against some gram-positive, acid-fast and gram-negative bacteria.

Alanine↗
PubMed1975

Isolation of a new peptide antibiotic complex 61-26. Studies on antibiotics from the geneus Bacillus. V.

A new antibiotic named 61-26 active against gram-positive bacteria and some fungi was isolated from a Bacillus strain. The antibiotic is a weakly basic peptide slightly soluble in aqueous alcohols. An approximate empirical formula of C50H93N11O17 and constituent amino acids of aspartic acid (1 mole), serine(2 moles), alanine (2moles), and sum of valine and isoleucine (2 moles) are indicated.

Alanine↗
PubMed1975

Isolation of two new related peptide antibiotics, cerexins A and B (studies on antibiotics from the genus Bacillus. I).

Two new antibiotics cerexins A and B were isolated from different strains identified with Bacillus cereus. These two antibiotics are amphoteric in nature, soluble in particular solvents such as dimethylsulfoxide, dimethylformamide and alkaline water, and show typical infrared absorptions of peptide. These also have similar antimicrobial properties active against gram-postive bacteria.

Animals↗
PubMed1975

Chemical characterization of new antibiotics, cerexins A and B. (Studies on antibiotics from the genus Bacillus. II)

Acid hydrolysis revealed that the antibiotic cerexin A is constructed with aspartic acid (3), threonine (1), serine (1), valine (2), allo-isoleucine (1), gamma-hydroxylysine (1), tryptophan (1), and a variety of fatty acid residues. The essential difference between cerexins A and B is concluded to be replacement of serine and one valine residue in cerexin A by glycine and phenylalanine in cerexin B. Isolation of a new amino acid L-threo-gamma-hydroxylysine is also described.

Anti-Bacterial Agents↗
PubMed1975

The amino acid sequence of cerexin A (studies on antibiotics from the genus Bacillus. VII.

N-Bromosuccinimide cleavage reaction on cerexin A liberated allo-isoleucine. Treatment with conc. hydrochloric acid cleaved the antibiotic into two peptide fragments selectively at gamma-hydroxylysine residue. Deacylation with an enzyme preparation from Pseudomonas sp. afforded deacyl cerexin A. The amino acid sequences of these peptide fragments were examined by Edman degradation. From all the results, the entire amino acid sequence of cerexin A was deduced.

Amino Acid Sequence↗