@article{oai:fukuyama-u.repo.nii.ac.jp:00007970,
 author = {楠瀬, 正道 and 菊田, 安至},
 issue = {2},
 journal = {福山大学工学部紀要},
 month = {Mar},
 note = {P(論文), We have isolated and sequenced cDNAs encoding two human leukotriene B_4 (LTB_4) ω-hydroxylases. Human neutrophil enzyme (CYP4F3) contained 520 amino acids with a molecular weight of 59,805 Da, while human liver enzyme (CYP4F2) contained 520 amino acids with a molecular weight of 59,853 Da. The two enzymes showed 87.3% sequence homology with each other. The microsomes from yeast cells transfected with the cDNAs for CYP4F3 and CYP4F2 catalyzed the ω-hydroxylation of LTB_4 with Km values of 0.71μM and 46μM, respectively. Highly purified enzyme of CYP4F3 also exhibited ω-hydroxylase activities toward LTB_4, 6-trans-LTB_4, 20-hydroxy LTB_4, lipoxin A_4, lipoxin B_4, and 12-HETE. Sourthern blot of human genomic DNA probed with the CYP4F3 cDNA indicated the existence of at least 5 related genes of CYP4F. The CYP4F3 gene, which contained 12 exons, was mapped to chromosome 19p13.2.},
 pages = {61--69},
 title = {ロイコトリエンB_4ω水酸化酵素の研究},
 volume = {19},
 year = {1996}
}