Search Results - "Fukasawa, K M"

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    Characterization of the Metal-Substituted Dipeptidyl Peptidase III (Rat Liver) by Hirose, Junzo, Iwamoto, Hiroyuki, Nagao, Ikuko, Enmyo, Kanako, Sugao, Hidenori, Kanemitu, Nobuharu, Ikeda, Keiichi, Takeda, Mitsunori, Inoue, Masaki, Ikeda, Tomoyuki, Matsuura, Fumito, Fukasawa, Kayoko M, Fukasawa, Katsuhiko

    Published in Biochemistry (Easton) (02-10-2001)
    “…Dipeptidyl peptidase III (DPP III) (EC 3.4.14.4), which has a HELLGH-E (residues 450−455, 508) motif as the zinc binding site, is classified as a zinc…”
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    Cloning and functional expression of rat kidney dipeptidyl peptidase II by Fukasawa, K M, Fukasawa, K, Higaki, K, Shiina, N, Ohno, M, Ito, S, Otogoto, J, Ota, N

    Published in Biochemical journal (15-01-2001)
    “…Dipeptidyl peptidase II (DPP II; EC 3.4.14.2) from rat kidney was purified to a specific activity of 65.4 micromol/min per mg of protein for…”
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  3. 3

    Differential expression of immune-modulatory molecule HLA-E in non-neoplastic and neoplastic lesions of the thyroid by Zanetti, B R, Carvalho-Galano, D F, Feitosa, N L F, Hassumi-Fukasawa, M K, Miranda-Camargo, F A, Maciel, L M Z, Ribeiro-Silva, A, Soares, E G

    “…Human leukocyte antigen (HLA)–E is a non-classical molecule of the histocompatibility complex that functions as one of the main ligands of the Natural Killer…”
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  4. 4

    Complete nucleotide sequence of the mouse lactate dehydrogenase-A functional gene: comparison of the exon-intron organization of dehydrogenase genes by Fukasawa, Kayoko M, Li, Steven S.-L

    Published in Genetics (Austin) (01-05-1987)
    “…The complete sequence of 12,851 nucleotides of the mouse lactate dehydrogenase-A (LDH-A) gene has been determined. It includes eight exons, seven introns,…”
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  5. 5

    Immunohistochemical localization of dipeptidyl aminopeptidase IV in rat kidney, liver, and salivary glands by Fukasawa, KM, Fukasawa, K, Sahara, N, Harada, M, Kondo, Y, Nagatsu, I

    “…Specific antibodies directed against dipeptidyl aminopeptidase (DAP) IV prepared from rat and pig kidneys were produced in rabbits. Using a peroxidase-labeled…”
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    The HELLGH Motif of Rat Liver Dipeptidyl Peptidase III Is Involved in Zinc Coordination and the Catalytic Activity of the Enzyme by Fukasawa, Katsuhiko, Fukasawa, Kayoko M, Iwamoto, Hiroyuki, Hirose, Junzo, Harada, Minoru

    Published in Biochemistry (Easton) (29-06-1999)
    “…The role of the HELLGH (residues 450−455) motif in the sequence of rat dipeptidyl peptidase III (EC 3.4.14.4) was investigated by replacing Glu451 with an…”
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  7. 7

    Molecular evolution of mammalian lactate dehydrogenase-A genes and pseudogenes: association of a mouse processed pseudogene with a B1 repetitive sequence by FUKASAWA, K. M, WEN-HSIUNG LI, YAGI, K, CHI-CHENG LUO, LI, S S.-L

    Published in Molecular biology and evolution (01-07-1986)
    “…A mouse genomic clone containing a lactate dehydrogenase-A (LDH-A) processed pseudogene and a B1 repetitive element was isolated, and a nucleotide sequence of…”
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  8. 8

    Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression by Fukasawa, K, Fukasawa, K M, Kanai, M, Fujii, S, Hirose, J, Harada, M

    Published in Biochemical journal (15-01-1998)
    “…We have purified dipeptidyl peptidase III (EC 3.4.14.4) from human placenta. It had a pH optimum of 8.8 and readily hydrolysed Arg-Arg-beta-naphthylamide…”
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    Nucleotide sequence of the putative regulatory region of mouse lactate dehydrogenase-A gene by Fukasawa, K M, Li, S S

    Published in Biochemical journal (15-04-1986)
    “…The nucleotide sequence of approx. 3 kilobases including the regulatory region, a non-coding exon and the first protein-coding exon from mouse lactate…”
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  11. 11

    Molecular Nature of Spontaneous Mutations in Mouse Lactate Dehydrogenase-A Processed Pseudogenes by Fukasawa, Kayoko M, Tanimura, Masako, Sakai, Ikuya, Sharief, Farida S, Chung, Fu-Zon, Li, Steven S.-L

    Published in Genetics (Austin) (01-01-1987)
    “…The presence of at least ten mouse LDH-A pseudogenes was demonstrated in the genomic blot analysis, and four different processed pseudogenes have thus far been…”
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  12. 12

    Molecular Cloning and Expression of Rat Liver Aminopeptidase B by Fukasawa, Kayoko M., Fukasawa, Katsuhiko, Kanai, Makoto, Fujii, Shingo, Harada, Minoru

    Published in The Journal of biological chemistry (29-11-1996)
    “…We isolated, by immunological screening of a Uni-ZAP XR cDNA library constructed from rat liver mRNAs, a cDNA clone with 2212 base pairs encoding…”
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  13. 13

    Characterization of a soluble form of dipeptidyl peptidase IV from pig liver by Fukasawa, K M, Fukasawa, K, Hiraoka, B Y, Harada, M

    Published in Experientia (01-01-1983)
    “…Soluble dipeptidyl peptidase IV (EC 3.4.14.5) was purified from the 100,000 X g supernatant fraction of pig liver homogenate. The purified enzyme had the same…”
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  14. 14

    Chemical modification of dipeptidyl peptidase iv: involvement of an essential tryptophan residue at the substrate binding site by Harada, M, Hiraoka, B Y, Fukasawa, K M, Fukasawa, K

    Published in Archives of biochemistry and biophysics (01-11-1984)
    “…Inactivation of pig kidney dipeptidyl peptidase IV (EC 3.4.14.5) by photosensitization in the presence of methylene blue at pH 7.5 was observed to have…”
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    Immunohistochemical localization of dipeptidyl aminopeptidase (DAP) IV in the rat submandibular gland during postnatal development by Sahara, N, Fukasawa, K M, Fukasawa, K, Araki, N, Suzuki, K

    Published in Histochemistry (1981)
    “…The localization of dipeptidyl aminopeptidase (DAP) IV in the rat submandibular gland during postnatal development was studied immunohistochemically using the…”
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  16. 16

    Phosphoprotein phosphatase activity of bovine intestinal alkaline phosphatase by Harada, M, Hiraoka, B Y, Fukasawa, K, Fukasawa, K M

    Published in Experientia (01-06-1981)
    “…The phosphoprotein phosphatase activity of a commercial preparation of bovine intestinal alkaline phosphatase (EC 3.1.3.1) was examined using phosvitin and…”
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  17. 17

    Purification, partial sequencing and characterization of an insect membrane dipeptidyl aminopeptidase that degrades the insect neuropeptide proctolin by Mazzocco, Claire, Fukasawa, Kayoko M., Raymond, Anne‐Aurélie, Puiroux, Jacques

    Published in European journal of biochemistry (01-09-2001)
    “…Two proctolin‐binding proteins solubilized from 1600 cockroach hindgut membranes were purified 1000‐fold using five chromatography steps. Twenty‐five…”
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