Bioscience, biotechnology, and biochemistry.
Publisher:
Japan Society for Bioscience, Biotechnology, and Agrochemistry,. Oxford : Oxford University Press (2021)
Frequency: Monthly
Country: England
Language: English
Author(s):
Nihon Nōgei Kagakkai.
Start Year:1992 -
ISSN:
0916-8451 (Print)
1347-6947 (Electronic)
0916-8451 (Linking)
1347-6947 (Electronic)
0916-8451 (Linking)
Impact Factor
1.6
2022
| NLM ID: | 9205717 |
| (DNLM): | SR0073164(s) |
| (OCoLC): | 25516229 |
| Coden: | BBBIEJ |
| Classification: | W1 BI91H |
Comparison of the efficacy of alpha-lactalbumin from equine, bovine, and human milk in the growth of intestinal IEC-6 cells. Native alpha-lactalbumins (α-LA) from equine, bovine, and human milk were not cytotoxic. However, after treatment with trifluoroethanol (TFE), all three α-LAs exhibited cytotoxicity. Toxic potencies were distinctly different among them. Equine α-LA was the most robust, bovine α-LA was moderate, and human α-LA was weak. There were no significant structural changes as between the native and the TFE-treated α-LAs.
Characterization and structure analysis of a novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14. A novel bacteriocin, lacticin Z, produced by Lactococcus lactis QU 14 isolated from a horse's intestinal tract was identified. Lacticin Z was purified through a three step procedure comprised of hydrophobic-interaction, cation-exchange chromatography, and reverse-phase HPLC. ESI-TOF MS determined the molecular mass of lacticin Z to be 5,968.9 Da. The primary structure of lacticin Z was found to consist of 53 amino acid residues without any leader sequence or signal peptide. Lacticin Z showed homology to lacticin Q from L. lactis QU 5, aureocin A53 from Staphylococcus aureus A53, and mutacin BH...
Appearance of nitrite reducing activity of cytochrome c upon heat denaturation. The appearance of NO2- reducing activity of cytochrome c (Cyt c) upon heat denaturation was investigated with equine heart Cyt c. Denatured equine heart Cyt c (dCyt c), which was treated at 100 degrees C for 30 min, had NO2- reducing activity in the presence of dithionite and methylviologen in an aqueous solution under anaerobic conditions. In contrast, hemoglobin and myoglobin had no such activity under the same conditions. Using spectroscopic methods, we found that the appearance of this activity in the Cyt c was due to the following intramolecular changes: unfolding of the peptide chain, ex...