Search PubMed⌕ Search

Biomedical subjects

T Katayama

Publications and source records attributed to T Katayama.

At least 577 records · Page 32Linked to original sources
PubMed1977

Dihydrotestosterone-binding protein in cytosols of normal and hypertrophic human prostates, and influence of estrogens and anti-androgens on the binding.

Dihydrotestosterone-binding protein was observed in cytosols of the normal and hypertrophic human prostates. Association constant for dihydrotestosterone of cytosol of the normal prostate differed slightly from that of the hypertrophic prostate. However, maximum binding capacity was almost identical in these tissues. No distinct correlation was detected between proportion of glandular constituent and binding characteristics (Ka and maximum binding capacity) in the hypertrophic prostates. Influence of some steroids on the binding with dihydrotesterone was examined. Testosterone, estradiol-17beta, estriol, cyproterone acetate and SK & F 7690 inhibited the binding competitively. However, Sch 13521 did not exhibit any influence on the binding.

Binding, Competitive↗
PubMed1977

Pholipomycin, a new member of phosphoglycolipid antibiotics. III. Biological properties.

Pholipomycin, a new member of the phosphoglycolipid antibiotics, was primarily active against gram-positive bacteria including clinically isolated resistant bacteria. It differed from other members of the antibiotic family as it also demonstrated activity against gram-negative bacteria. Pholipomycin protected mice from infection with Staphylococcus aureus and was nontoxic to mice having an LD50 (i.v.) of 600 mg/kg. Besides possessing anti-microbiol activity, pholipomycin, when administered orally, appeared to promote growth in chickens and pigs.

Actinomycetales↗
PubMed1976

Isolation and purification of D-alanyl-meso-2, 6-diaminopimelic acid endopeptidase of Streptomyces L-3 enzyme using soluble substrates of known chemical structure from Lactobacillus plantarum cell wall digests.

D-alanyl-meso-2, 6-diaminopimelic acid (D-Alanyl-meso-A2pm) endopeptidase was isolated and purified from a crude Streptomyces L-3 enzyme preparation by ion exchange chromatography and isoelectric focusing in a density gradient. During its purification, its hydrolytic activity was assayed on cell walls of Lactobacillus plantarum ATCC 8014 and soluble glycopeptides and peptides, of known chemical structures, prepared enzymatically from these cell walls. A fraction with an isoelectric point of pH 7.9 cleaved the bond between the carboxyl group of the D-alanine residue at the C-terminal in one peptide subunit and one of the two amino groups of the A2pm residue in the neighboring peptide subunit. Unlike the crude enzyme, the endopeptidase in this fraction showed no N-acetylmuramyl-L-alanine amidase, A2pm carboxyamide amidase or proteinase(s) activity and it was immunologically homogeneous.

Alanine↗