Zobrazeno 1 - 10
of 131
pro vyhledávání: '"Hiroh Ikezawa"'
Publikováno v:
Archives of Biochemistry and Biophysics. 436:227-236
Sphingomyelinase (SMase) from Bacillus cereus has been known to be activated by Mg 2+ , Mn 2+ , and Co 2+ , but strongly inhibited by Zn 2+ . In the present study, we investigated the effects of several kinds of metal ions on the catalytic activity o
Autor:
Hiroh Ikezawa
Publikováno v:
Journal of Toxicology: Toxin Reviews. 23:479-508
Bacterial phosphatidylinositol‐specific phospholipases C have been shown not only to cause breakdown of phosphatidylinositol but also to release GPI‐anchored proteins from the plasma membranes of eucaryotes. Several enzymes in this group have bee
Publikováno v:
Journal of Biochemistry. 133:279-286
Bacillus cereus sphingomyelinase (SMase) is an extracellular hemolysin classified into a group of Mg(2+)-dependent neutral SMases (nSMase). Sequence comparison of bacterial and eukaryotic Mg(2+)-dependent nSMases has shown that several amino acid res
Autor:
Masayoshi Imagawa, Hiroh Ikezawa, Kikuo Tsukamoto, Shinobu Fujii, Kiyoshi Ikeda, Takashi Obama
Publikováno v:
Biological and Pharmaceutical Bulletin. 26:920-926
Bacillus cereus sphingomyelinase belongs to the Mg(2+)-dependent neutral sphingomyelinase, which hydrolyses sphingomyelin to phosphocholine and ceramide, and acts as an extracellular hemolysin. The triplet residues, His151-Asp195-His296, of the enzym
Autor:
Hiroh Ikezawa
Publikováno v:
Biological and Pharmaceutical Bulletin. 25:409-417
From the numerous studies developed at the last quarter of the 20th century, glycosylphosphatidylinositol (GPI) anchor has been established as a unique mode of protein binding to the plasma membrane. The core structure of this anchor consists of etha
Autor:
Hiroe Honda, Yasukazu Oomoto, Takemasa Takii, Hiroh Ikezawa, Kikuo Onozaki, Tomoko Kobayashi, Shigezo Udaka, Satoshi Sasayama
Publikováno v:
Journal of Interferon & Cytokine Research. 19:1325-1331
Interleukin-1 receptor antagonist (IL-1RA) has been used as a tool to study the biologic activity of IL-1 and as a possible therapeutic substance for inflammatory disease. To perform in vivo study, however, large quantities of IL-1RA are required. Ba
Autor:
Tetsuyuki Kobayashi, Hiroh Ikezawa, Rieko Tanaka-Ishii, Ryo Taguchi, Kimiko Murakami-Murofushi
Publikováno v:
Life Sciences. 65:2185-2191
A novel bioactive lipid, cyclic phosphatidic acid (cPA), was identified in lipids bound to human serum albumin. A cPA fraction was extracted and purified from human serum albumin by use of a combination of preparative TLC and HPLC. Electrospray ioniz
Autor:
Hideo Nakano, Hiroh Ikezawa, Yugo Iwasaki, Tomoko Kobayashi, Tsuneo Yamane, Akiko Ichihashi, Yukiko Tsubouchi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1391:52-66
Two phosphatidylinositol-specific phospholipase C (PI-PLC) genes from Streptomyces antibioticus were cloned by a shotgun method using Streptomyces lividans TK24 as a host. The genes of the two PI-PLCs (named as PLC1 and PLC2) were adjoined and opposi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1328:185-196
Bovine liver 5′-nucleotidase is a GPI-anchored protein whose Ser523 attaches to GPI as the ω-site. For GPI-modification, pro-protein of the enzyme possesses a signal peptide at the C-terminus, comprising a hydrophilic spacer sequence of 8 amino ac
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1334:1-4
GPI-anchored proteins are distributed ubiquitously in eukaryotes, but not in procaryotes. By methabolic-labeling of Sulfolobus acidocaldarius cells, 14C-radiolabeled precursors of GPI and caldarchaetidylinositol were incorporated into 120, 143 and 18