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Biomedical subjects

D S Slusarchyk

Publications and source records attributed to D S Slusarchyk.

10 recordsLinked to original sources
PubMed1987

Xylocandin: a new complex of antifungal peptides. I. Taxonomy, isolation and biological activity.

Xylocandin is a complex of novel peptides with potent antifungal activity that is produced by Pseudomonas cepacia ATCC 39277. The complex was isolated from the fermentation broth by extraction with butanol-methanol, 9:1, followed by collection of the precipitate formed upon concentration of the solvent extract. Purification was effected by chromatography on reversed phase and size exclusion gels followed by TLC on silica gel. These techniques afforded eight components: A1, A2, B1, B2, C1, C2, D1 and D2. A mixture of the two closely related components, xylocandins A1 and A2, displayed potent anticandidal and antidermatophytic activities in vitro. The activity was diminished by the presence of serum or vaginal washings. No antibacterial activity was demonstrable.

Animals↗
PubMed1985

Catacandins, novel anticandidal antibiotics of bacterial origin.

Two novel antibiotics, catacandin A and catacandin B, were isolated from the fermentation broth of the bacterium, Lysobacter gummosus, by extraction and adsorption, reverse-phase and gel filtration chromatography. On the basis of their physico-chemical properties, they are acyltetramic acids that are easily distinguishable from others in this class. Catacandin A and catacandin B possess good anticandidal activity.

Anti-Bacterial Agents↗
PubMed1984

Phenacein--an angiotensin-converting enzyme inhibitor produced by a streptomycete. I. Taxonomy, fermentation and biological properties.

Phanacein, 3,6-dihydroxy-1-phenazinecarboxylic acid, was a specific angiotensin-converting enzyme (ACE) inhibitor isolated from a member of the Streptomyces tanashiensis-zaomyceticus group. Phenacein acted as a pure competitive inhibitor with a Ki of 0.58 microM. ACE inhibition could be reversed by Zn++, but not by Co++, Ca++, or Mg++; therefore, phenacein may chelate the active site zinc of ACE. However, other zinc-containing enzymes were not inhibited at high phenacein concentrations. Phenacein exhibited weak activity against Gram-positive bacteria, but was not active against Candida sp. or Gram-negative organisms.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1984

Muraceins--muramyl peptides produced by Nocardia orientalis as angiotensin-converting enzyme inhibitors. I. Taxonomy, fermentation and biological properties.

Three muraceins , a family of muramyl peptides, were isolated from Nocardia orientalis as inhibitors of angiotensin-converting enzyme (ACE). Muracein A, the most potent inhibitor, inhibited ACE competitively with a Ki of 1.5 microM. Liver alcohol dehydrogenase and carboxypeptidase A, two other zinc-containing enzymes, were not inhibited at 150 microM. Inhibition of ACE could not be reversed by divalent cations.

Acetylmuramyl-Alanyl-Isoglutamine↗
PubMed1982

Activity of sulfa drugs and dihydrofolate reductase inhibitors against Candida albicans.

Growth of Candida albicans can be inhibited by sulfa drugs which prevent biosynthesis of folic acid. The dihydrofolate reductase (E.C. 1.5.1.3) inhibitors aminopterin and methotrexate also exhibit anticandidal activity, but trimethoprim does not. Kinetic evaluations with C. albicans dihydrofolate reductase indicate that methotrexate and aminopterin are tight-binding inhibitors whereas trimethoprim binds poorly.

Aminopterin↗
PubMed1978

Ionomycin, a new polyether antibiotic.

Ionomycin, a new polyether antibiotic with a high affinity for calcium ions, is obtained in pure form from fermentation broths of Streptomyces conglobatus sp. nov. Trejo by solvent extraction. It is unique amongst known polyether antibiotics in that it has a UV absorption maximum at 300 nm. thereby distinguishing it from other antibiotics of its class. The Ca salt has the molecular formula C41H70O9Ca. Ionomycin is a narrow spectrum antibiotic being active against Gram-positive bacteria.

Animals↗